A conserved mechanism drives partition complex assembly on bacterial chromosomes and plasmids

Chromosome and plasmid segregation in bacteria are mostly driven by ParAB S systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites ( parS ). However, the mechanism of how a few parS ‐bound ParB proteins nucleate the formation of highly concent...

Full description

Saved in:
Bibliographic Details
Published inMolecular systems biology Vol. 14; no. 11; pp. e8516 - n/a
Main Authors Debaugny, Roxanne E, Sanchez, Aurore, Rech, Jérôme, Labourdette, Delphine, Dorignac, Jérôme, Geniet, Frédéric, Palmeri, John, Parmeggiani, Andrea, Boudsocq, François, Anton Leberre, Véronique, Walter, Jean‐Charles, Bouet, Jean‐Yves
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.11.2018
EMBO Press
John Wiley and Sons Inc
Springer Nature
Subjects
Adenosine triphosphatase
Assembly
Bacteria
Bacterial Proteins - metabolism
Bacteriology
Binding
Biochemistry, Molecular Biology
Biological Physics
Chromosome Segregation
Chromosomes
Chromosomes, Bacterial - genetics
Chromosomes, Bacterial - physiology
Coding
Deoxyribonucleic acid
DNA
DNA segregation
E coli
EMBO13
EMBO23
EMBO33
Escherichia coli
F plasmid
Life Sciences
Mathematical models
Microbiology and Parasitology
Models, Theoretical
Nucleation
ParABS
Partitions
Physics
plasmid partition
Plasmids
Plasmids - genetics
Plasmids - physiology
Proteins
Robustness (mathematics)
Stochastic Processes
Stochasticity
Systems Biology - methods
Transcription
Vibrio cholerae - metabolism
Vibrio cholerae - physiology
Waterborne diseases
DNA segregation
F plasmid
ParABS
plasmid partition
Escherichia coli
Online AccessGet full text

Cover

Abstract Chromosome and plasmid segregation in bacteria are mostly driven by ParAB S systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites ( parS ). However, the mechanism of how a few parS ‐bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico‐mathematical models. We discriminated between these different models by varying some key parameters in vivo using the F plasmid partition system. We found that “Nucleation & caging” is the only coherent model recapitulating in vivo data. We also showed that the stochastic self‐assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATPase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the “Nucleation & caging” model and successfully applied it to the chromosomally encoded Par system of Vibrio cholerae , indicating that this stochastic self‐assembly mechanism is widely conserved from plasmids to chromosomes. Synopsis High‐resolution ChIP‐seq and physico‐mathematical modeling are used to analyze the in vivo ParB DNA‐binding profiles. The “Nucleation and caging” self‐assembly mechanism is widespread to ensure faithful bacterial DNA segregation by ParAB S systems. ParB S partition complexes are highly dynamic nucleoprotein complexes. The robust ParB DNA binding profiles derived by ChIP‐seq data are well‐described by the “Nucleation and caging” model. The size of the partition complex is invariant to intracellular variation in ParB levels. This self‐assembly mechanism is observed on Escherichia coli and V. cholerae chromosomes and on the F plasmid. Graphical Abstract High‐resolution ChIP‐seq and physico‐mathematical modeling are used to analyze the in vivo ParB DNA‐binding profiles. The “Nucleation and caging” self‐assembly mechanism is widespread to ensure faithful bacterial DNA segregation by ParAB S systems.
AbstractList Chromosome and plasmid segregation in bacteria are mostly driven by ParAB S systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites ( parS ). However, the mechanism of how a few parS ‐bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico‐mathematical models. We discriminated between these different models by varying some key parameters in vivo using the F plasmid partition system. We found that “Nucleation & caging” is the only coherent model recapitulating in vivo data. We also showed that the stochastic self‐assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATPase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the “Nucleation & caging” model and successfully applied it to the chromosomally encoded Par system of Vibrio cholerae , indicating that this stochastic self‐assembly mechanism is widely conserved from plasmids to chromosomes. Synopsis High‐resolution ChIP‐seq and physico‐mathematical modeling are used to analyze the in vivo ParB DNA‐binding profiles. The “Nucleation and caging” self‐assembly mechanism is widespread to ensure faithful bacterial DNA segregation by ParAB S systems. ParB S partition complexes are highly dynamic nucleoprotein complexes. The robust ParB DNA binding profiles derived by ChIP‐seq data are well‐described by the “Nucleation and caging” model. The size of the partition complex is invariant to intracellular variation in ParB levels. This self‐assembly mechanism is observed on Escherichia coli and V. cholerae chromosomes and on the F plasmid. Graphical Abstract High‐resolution ChIP‐seq and physico‐mathematical modeling are used to analyze the in vivo ParB DNA‐binding profiles. The “Nucleation and caging” self‐assembly mechanism is widespread to ensure faithful bacterial DNA segregation by ParAB S systems.
Chromosome and plasmid segregation in bacteria are mostly driven by ParABS systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites (parS). However, the mechanism of how a few parS‐bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico‐mathematical models. We discriminated between these different models by varying some key parameters in vivo using the F plasmid partition system. We found that “Nucleation & caging” is the only coherent model recapitulating in vivo data. We also showed that the stochastic self‐assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATPase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the “Nucleation & caging” model and successfully applied it to the chromosomally encoded Par system of Vibrio cholerae, indicating that this stochastic self‐assembly mechanism is widely conserved from plasmids to chromosomes. Synopsis High‐resolution ChIP‐seq and physico‐mathematical modeling are used to analyze the in vivo ParB DNA‐binding profiles. The “Nucleation and caging” self‐assembly mechanism is widespread to ensure faithful bacterial DNA segregation by ParABS systems. ParBS partition complexes are highly dynamic nucleoprotein complexes. The robust ParB DNA binding profiles derived by ChIP‐seq data are well‐described by the “Nucleation and caging” model. The size of the partition complex is invariant to intracellular variation in ParB levels. This self‐assembly mechanism is observed on Escherichia coli and V. cholerae chromosomes and on the F plasmid. High‐resolution ChIP‐seq and physico‐mathematical modeling are used to analyze the in vivo ParB DNA‐binding profiles. The “Nucleation and caging” self‐assembly mechanism is widespread to ensure faithful bacterial DNA segregation by ParABS systems.
Chromosome and plasmid segregation in bacteria are mostly driven by ParABS systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites (parS). However, the mechanism of how a few parS-bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico-mathematical models. We discriminated between these different models by varying some key parameters in vivo using the plasmid F partition system. We found that ‘Nucleation & caging’ is the only coherent model recapitulating in vivo data. We also showed that the stochastic self-assembly of partition complexes (i) does not directly involve ParA, (ii) results in a dynamic structure of discrete size independent of ParB concentration, and (iii) is not perturbed by active transcription but is by protein complexes. We refined the ‘Nucleation & Caging’ model and successfully applied it to the chromosomally-encoded Par system of Vibrio cholerae, indicating that this stochastic self-assembly mechanism is widely conserved from plasmids to chromosomes.
Chromosome and plasmid segregation in bacteria are mostly driven by ParABS systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites (parS). However, the mechanism of how a few parS-bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico-mathematical models. We discriminated between these different models by varying some key parameters in vivo using the F plasmid partition system. We found that "Nucleation & caging" is the only coherent model recapitulating in vivo data. We also showed that the stochastic self-assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATPase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the "Nucleation & caging" model and successfully applied it to the chromosomally encoded Par system of Vibrio cholerae, indicating that this stochastic self-assembly mechanism is widely conserved from plasmids to chromosomes.
Abstract Chromosome and plasmid segregation in bacteria are mostly driven by ParABS systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites (parS). However, the mechanism of how a few parS‐bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico‐mathematical models. We discriminated between these different models by varying some key parameters in vivo using the F plasmid partition system. We found that “Nucleation & caging” is the only coherent model recapitulating in vivo data. We also showed that the stochastic self‐assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATPase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the “Nucleation & caging” model and successfully applied it to the chromosomally encoded Par system of Vibrio cholerae, indicating that this stochastic self‐assembly mechanism is widely conserved from plasmids to chromosomes.
Chromosome and plasmid segregation in bacteria are mostly driven by ParAB systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites ( ). However, the mechanism of how a few -bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico-mathematical models. We discriminated between these different models by varying some key parameters using the F plasmid partition system. We found that "Nucleation & caging" is the only coherent model recapitulating data. We also showed that the stochastic self-assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATPase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the "Nucleation & caging" model and successfully applied it to the chromosomally encoded Par system of , indicating that this stochastic self-assembly mechanism is widely conserved from plasmids to chromosomes.
Chromosome and plasmid segregation in bacteria are mostly driven by ParAB S systems. These DNA partitioning machineries rely on large nucleoprotein complexes assembled on centromere sites ( parS ). However, the mechanism of how a few parS ‐bound ParB proteins nucleate the formation of highly concentrated ParB clusters remains unclear despite several proposed physico‐mathematical models. We discriminated between these different models by varying some key parameters in vivo using the F plasmid partition system. We found that “Nucleation & caging” is the only coherent model recapitulating in vivo data. We also showed that the stochastic self‐assembly of partition complexes (i) is a robust mechanism, (ii) does not directly involve ParA ATP ase, (iii) results in a dynamic structure of discrete size independent of ParB concentration, and (iv) is not perturbed by active transcription but is by protein complexes. We refined the “Nucleation & caging” model and successfully applied it to the chromosomally encoded Par system of Vibrio cholerae , indicating that this stochastic self‐assembly mechanism is widely conserved from plasmids to chromosomes.
Author Debaugny, Roxanne E
Dorignac, Jérôme
Labourdette, Delphine
Anton Leberre, Véronique
Rech, Jérôme
Geniet, Frédéric
Parmeggiani, Andrea
Walter, Jean‐Charles
Palmeri, John
Sanchez, Aurore
Boudsocq, François
Bouet, Jean‐Yves
AuthorAffiliation 2 LISBP CNRS INRA INSA Université de Toulouse Toulouse France
4 Dynamique des Interactions Membranaires Normales et Pathologiques CNRS‐Université Montpellier Montpellier France
3 Laboratoire Charles Coulomb CNRS‐Université Montpellier Montpellier France
1 Laboratoire de Microbiologie et Génétique Moléculaires Centre de Biologie Intégrative (CBI) Centre National de la Recherche Scientifique (CNRS) Université de Toulouse, UPS Toulouse France
5 Present address: Institut Curie UMR 3664 CNRS‐IC Paris France
AuthorAffiliation_xml – name: 3 Laboratoire Charles Coulomb CNRS‐Université Montpellier Montpellier France
– name: 4 Dynamique des Interactions Membranaires Normales et Pathologiques CNRS‐Université Montpellier Montpellier France
– name: 1 Laboratoire de Microbiologie et Génétique Moléculaires Centre de Biologie Intégrative (CBI) Centre National de la Recherche Scientifique (CNRS) Université de Toulouse, UPS Toulouse France
– name: 5 Present address: Institut Curie UMR 3664 CNRS‐IC Paris France
– name: 2 LISBP CNRS INRA INSA Université de Toulouse Toulouse France
Author_xml – sequence: 1
  givenname: Roxanne E
  surname: Debaugny
  fullname: Debaugny, Roxanne E
  organization: Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, UPS
– sequence: 2
  givenname: Aurore
  surname: Sanchez
  fullname: Sanchez, Aurore
  organization: Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, UPS, Institut Curie, UMR 3664 CNRS‐IC
– sequence: 3
  givenname: Jérôme
  surname: Rech
  fullname: Rech, Jérôme
  organization: Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, UPS
– sequence: 4
  givenname: Delphine
  surname: Labourdette
  fullname: Labourdette, Delphine
  organization: LISBP, CNRS, INRA, INSA, Université de Toulouse
– sequence: 5
  givenname: Jérôme
  surname: Dorignac
  fullname: Dorignac, Jérôme
  organization: Laboratoire Charles Coulomb, CNRS‐Université Montpellier
– sequence: 6
  givenname: Frédéric
  surname: Geniet
  fullname: Geniet, Frédéric
  organization: Laboratoire Charles Coulomb, CNRS‐Université Montpellier
– sequence: 7
  givenname: John
  surname: Palmeri
  fullname: Palmeri, John
  organization: Laboratoire Charles Coulomb, CNRS‐Université Montpellier
– sequence: 8
  givenname: Andrea
  surname: Parmeggiani
  fullname: Parmeggiani, Andrea
  organization: Laboratoire Charles Coulomb, CNRS‐Université Montpellier, Dynamique des Interactions Membranaires Normales et Pathologiques, CNRS‐Université Montpellier
– sequence: 9
  givenname: François
  surname: Boudsocq
  fullname: Boudsocq, François
  organization: Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, UPS
– sequence: 10
  givenname: Véronique
  surname: Anton Leberre
  fullname: Anton Leberre, Véronique
  organization: LISBP, CNRS, INRA, INSA, Université de Toulouse
– sequence: 11
  givenname: Jean‐Charles
  surname: Walter
  fullname: Walter, Jean‐Charles
  email: jean-charles.walter@umontpellier.fr
  organization: Laboratoire Charles Coulomb, CNRS‐Université Montpellier
– sequence: 12
  givenname: Jean‐Yves
  orcidid: 0000-0003-1488-5455
  surname: Bouet
  fullname: Bouet, Jean‐Yves
  email: jean-yves.bouet@ibcg.biotoul.fr
  organization: Laboratoire de Microbiologie et Génétique Moléculaires, Centre de Biologie Intégrative (CBI), Centre National de la Recherche Scientifique (CNRS), Université de Toulouse, UPS
BackLink https://www.ncbi.nlm.nih.gov/pubmed/30446599$$D View this record in MEDLINE/PubMed
https://hal.science/hal-01926457$$DView record in HAL
BookMark eNp9ks-PEyEUgCdmjftDj17NJF7cQyswwMDFpLtRd5MaD-rREApvWpoBKrTV_vdLd3br7sZ4gjy-9_EevNPqKMQAVfUaozFmhJH3Ps_GBGEhGObPqhPcUjqiRJKjB_vj6jTnJUKNwIK8qI4bRClnUp5UPye1iSFD2oKtPZiFDi772ia3hVyvdFq7tYuhQH7Vw59a5wx-1u_qEptps4bkdF-bRYo-5uhLjg62XvU6e2fzy-p5p_sMr-7Ws-rHp4_fL69G06-fry8n05HhpOUjKxAF1NIGOMZYog5ZkKJFmhvGhG460-KWE9baUr-wknUaYTQTkmIEmpLmrLoevDbqpVol53Xaqaidug3ENFf7TkwPijAjOmGBdVjTjgqBWoOJbCjSiGPGi-vD4FptZh6sgbBOun8kfXwS3ELN41ZxUp63kUVwPggWT9KuJlO1jyEsCaes3eLCvru7LMVfG8hr5V020Pc6QNxkRXDDMCm_tde-fYIu4yaF8qx7SmJCWrSnRgNlUsw5QXeoACN1OzCqDIy6H5jCv3nY7YG-n5AC0AH47XrY_d-mvny7OHjHQ1ouGWEO6W-1_y7kBi4e2tk
CitedBy_id crossref_primary_10_1016_j_ceb_2021_07_001
crossref_primary_10_3389_fbioe_2022_800734
crossref_primary_10_1016_j_cell_2019_11_015
crossref_primary_10_1128_ecosalplus_esp_0008_2022
crossref_primary_10_1016_j_bpj_2021_08_022
crossref_primary_10_7554_eLife_79480
crossref_primary_10_1016_j_jmb_2021_167401
crossref_primary_10_1128_ecosalplus_esp_0003_2019
crossref_primary_10_1016_j_molcel_2020_06_034
crossref_primary_10_1093_molbev_msz308
crossref_primary_10_1016_j_molcel_2021_09_004
crossref_primary_10_1093_nar_gkac651
crossref_primary_10_1093_nar_gkad982
crossref_primary_10_1103_PhysRevResearch_2_033377
crossref_primary_10_7554_eLife_81362
crossref_primary_10_1002_syst_202400011
crossref_primary_10_7554_eLife_53515
crossref_primary_10_1073_pnas_2319205121
crossref_primary_10_1093_nar_gkad868
crossref_primary_10_1021_jacs_4c04749
crossref_primary_10_1038_s12276_024_01226_x
crossref_primary_10_3389_fmicb_2021_751880
crossref_primary_10_1007_s00709_019_01442_7
crossref_primary_10_1126_sciadv_abn3299
crossref_primary_10_3390_mi13060914
crossref_primary_10_7554_eLife_43812
crossref_primary_10_1371_journal_pcbi_1008869
crossref_primary_10_1126_science_aaz8632
crossref_primary_10_1038_s41589_019_0339_x
crossref_primary_10_1016_j_isci_2020_101861
crossref_primary_10_1098_rsob_200097
crossref_primary_10_1038_s41467_020_15238_4
crossref_primary_10_1371_journal_pone_0226472
crossref_primary_10_3390_microorganisms8010105
crossref_primary_10_1038_s41467_023_40320_y
crossref_primary_10_1103_PhysRevLett_127_138101
crossref_primary_10_1002_adbi_201800316
crossref_primary_10_1016_j_bpj_2020_09_023
Cites_doi 10.1016/B978-0-12-407678-5.00002-7
10.1111/j.1365-2958.2006.05537.x
10.1201/9781134111589
10.1128/jb.176.11.3188-3195.1994
10.1073/pnas.120163297
10.1073/pnas.92.6.1896
10.1111/j.1365-2958.2004.04396.x
10.1074/jbc.M109.044800
10.1128/JB.00250-06
10.1128/mBio.01061-14
10.1073/pnas.1402529111
10.1074/jbc.275.11.8213
10.1046/j.1365-2958.2000.02101.x
10.1093/nar/gkx271
10.1088/1367-2630/aaad39
10.1073/pnas.91.17.8027
10.1201/b16269
10.1128/jb.165.3.1043-1045.1986
10.1101/gad.242206.114
10.1093/emboj/18.5.1415
10.1016/0022-2836(86)90459-6
10.1111/mmi.12017
10.1103/PhysRevLett.119.028101
10.1038/ncomms12107
10.1093/nar/gku1295
10.1016/j.bpj.2017.02.039
10.1371/journal.pgen.1006428
10.1016/j.cell.2013.11.028
10.1016/j.cels.2015.07.013
10.1371/journal.pgen.1003956
10.1074/jbc.271.29.17469
10.1046/j.1365-2958.2000.01975.x
10.1016/j.bpj.2009.11.002
10.1126/science.aaa9046
10.1016/j.cell.2008.07.044
10.1038/emboj.2013.34
10.1128/JB.187.17.6166-6174.2005
10.1016/S0021-9258(18)53738-8
10.1111/j.1365-2958.2010.07507.x
10.1111/j.1365-2958.2008.06465.x
10.1007/978-1-4939-7098-8_6
10.3389/fmolb.2016.00044
10.1111/j.1365-2958.2006.05316.x
10.1126/science.283.5401.546
10.1074/jbc.M802752200
10.7554/eLife.02758
10.7554/eLife.28086
10.1098/rsob.150263
10.1006/jmbi.1996.0326
10.1111/j.1365-2958.2004.04322.x
10.1016/S0092-8674(00)81135-6
10.1111/j.1365-2958.2007.05690.x
10.1093/nar/gkr457
10.1073/pnas.97.26.14656
10.1016/0022-2836(73)90434-8
10.1128/microbiolspec.PLAS-0023-2014
10.1093/nar/gkt018
10.1093/emboj/20.17.4901
10.1016/j.plasmid.2015.03.007
ContentType Journal Article
Copyright The Author(s) 2018
2018 The Authors. Published under the terms of the CC BY 4.0 license
2018 The Authors. Published under the terms of the CC BY 4.0 license.
2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Attribution
Copyright_xml – notice: The Author(s) 2018
– notice: 2018 The Authors. Published under the terms of the CC BY 4.0 license
– notice: 2018 The Authors. Published under the terms of the CC BY 4.0 license.
– notice: 2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: Attribution
DBID C6C
24P
WIN
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
3V.
7QL
7TM
7U9
7X7
7XB
88A
88E
8AO
8FD
8FE
8FH
8FI
8FJ
8FK
8G5
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
C1K
CCPQU
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
GUQSH
H94
HCIFZ
K9.
LK8
M0S
M1P
M2O
M7N
M7P
MBDVC
P64
PADUT
PIMPY
PQEST
PQQKQ
PQUKI
PRINS
Q9U
RC3
7X8
1XC
VOOES
5PM
DOA
DOI 10.15252/msb.20188516
DatabaseName SpringerOpen
Wiley Online Library (Open Access Collection)
Wiley Online Library
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
ProQuest Central (Corporate)
Bacteriology Abstracts (Microbiology B)
Nucleic Acids Abstracts
Virology and AIDS Abstracts
ProQuest Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Biology Database (Alumni Edition)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
Technology Research Database
ProQuest SciTech Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Research Library (Alumni Edition)
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
ProQuest Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Central
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
Research Library Prep
AIDS and Cancer Research Abstracts
SciTech Premium Collection (Proquest) (PQ_SDU_P3)
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
ProQuest Research Library
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biological Science Database
Research Library (Corporate)
Biotechnology and BioEngineering Abstracts
Research Library China
Access via ProQuest (Open Access)
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
ProQuest Central Basic
Genetics Abstracts
MEDLINE - Academic
Hyper Article en Ligne (HAL)
Hyper Article en Ligne (HAL) (Open Access)
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Publicly Available Content Database
Research Library Prep
ProQuest Central Student
Technology Research Database
ProQuest Central Essentials
Nucleic Acids Abstracts
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
Research Library (Alumni Edition)
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central China
Environmental Sciences and Pollution Management
ProQuest Biology Journals (Alumni Edition)
ProQuest Central
Genetics Abstracts
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
Natural Science Collection
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biological Science Collection
AIDS and Cancer Research Abstracts
ProQuest Research Library
Research Library China
ProQuest Medical Library (Alumni)
Virology and AIDS Abstracts
ProQuest Biological Science Collection
ProQuest Central Basic
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
Biological Science Database
ProQuest SciTech Collection
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
Engineering Research Database
ProQuest One Academic
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList


MEDLINE - Academic
Publicly Available Content Database

MEDLINE
Database_xml – sequence: 1
  dbid: C6C
  name: SpringerOpen
  url: http://www.springeropen.com/
  sourceTypes: Publisher
– sequence: 2
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 3
  dbid: 24P
  name: Wiley Online Library (Open Access Collection)
  url: https://authorservices.wiley.com/open-science/open-access/browse-journals.html
  sourceTypes: Publisher
– sequence: 4
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 5
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 6
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
Physics
DocumentTitleAlternate Roxanne E Debaugny et al
EISSN 1744-4292
EndPage n/a
ExternalDocumentID oai_doaj_org_article_25c8f8de5f1a4f48807c129340a06156
oai_HAL_hal_01926457v1
10_15252_msb_20188516
30446599
MSB188516
Genre article
Research Support, Non-U.S. Gov't
Journal Article
GrantInformation_xml – fundername: Agence Nationale de la Recherche (ANR)
  grantid: ANR‐14‐CE09‐0025‐01
  funderid: 10.13039/501100001665
– fundername: Université de Toulouse
  grantid: APR14
– fundername: Labex NUMEV
  grantid: AAP 2013‐2‐005; 2015‐2‐055; 2016‐1‐024
– fundername: Centre National de la Recherche Scientifique (CNRS)
  funderid: 10.13039/501100004794
– fundername: Agence Nationale de la Recherche (ANR)
  funderid: ANR‐14‐CE09‐0025‐01
– fundername: Labex NUMEV
  funderid: AAP 2013‐2‐005; 2015‐2‐055; 2016‐1‐024
– fundername: Centre National de la Recherche Scientifique (CNRS)
– fundername: Université de Toulouse
  funderid: APR14
– fundername: Agence Nationale de la Recherche (ANR)
  grantid: ANR‐14‐CE09‐0025‐01
GroupedDBID ---
-Q-
0R~
123
1OC
24P
29M
2WC
39C
3V.
53G
5VS
7X7
88E
8AO
8FE
8FH
8FI
8FJ
8G5
8R4
8R5
AAHHS
ABDBF
ABUWG
ACCFJ
ACGFO
ACPRK
ACXQS
ADBBV
ADKYN
ADRAZ
ADZMN
AEEZP
AEGXH
AENEX
AEQDE
AFKRA
AFRAH
AHMBA
AIAGR
AIWBW
AJBDE
ALIPV
ALMA_UNASSIGNED_HOLDINGS
ALUQN
AOIJS
AVUZU
AZFZN
AZQEC
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
BPHCQ
BVXVI
C6C
CAG
CCPQU
CS3
DIK
DU5
DWQXO
E3Z
EBD
EBS
EJD
EMB
EMOBN
ESX
F5P
FYUFA
GNUQQ
GROUPED_DOAJ
GUQSH
GX1
HCIFZ
HH5
HK~
HMCUK
HYE
HZ~
IAO
IHR
INH
KQ8
LK8
M1P
M2O
M48
M7P
ML0
M~E
O5R
O5S
O9-
OK1
P2P
PADUT
PIMPY
PQQKQ
PSQYO
Q2X
RHI
RNS
RNTTT
RPM
SV3
TR2
TUS
UKHRP
WIN
WOQ
WOW
XSB
~8M
4.4
88A
ACSMW
COF
EBLON
GODZA
H13
IGS
M0L
PROAC
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
ITC
7QL
7TM
7U9
7XB
8FD
8FK
C1K
FR3
H94
K9.
M7N
MBDVC
P64
PQEST
PQUKI
PRINS
Q9U
RC3
7X8
1XC
VOOES
5PM
ID FETCH-LOGICAL-c6276-d804e0743e611190f0de9870a6c558a3fc7176257d8188d95fa010b89410ea423
IEDL.DBID RPM
ISSN 1744-4292
IngestDate Mon Nov 04 19:56:17 EST 2024
Tue Sep 17 21:03:10 EDT 2024
Thu Oct 17 06:45:12 EDT 2024
Sat Oct 26 05:47:49 EDT 2024
Thu Oct 10 20:35:36 EDT 2024
Thu Sep 26 17:04:45 EDT 2024
Sat Nov 02 12:16:40 EDT 2024
Sat Aug 24 00:45:37 EDT 2024
Fri Oct 25 01:30:25 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 11
Keywords DNA segregation
F plasmid
ParABS
plasmid partition
Escherichia coli
Language English
License Attribution
2018 The Authors. Published under the terms of the CC BY 4.0 license.
Attribution: http://creativecommons.org/licenses/by
This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c6276-d804e0743e611190f0de9870a6c558a3fc7176257d8188d95fa010b89410ea423
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000-0003-1488-5455
0000-0002-7313-0100
0009-0000-8949-2379
0000-0002-8022-4295
0000-0002-1599-3450
0000-0002-1015-528X
0000-0001-6337-0955
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6238139/
PMID 30446599
PQID 2139122709
PQPubID 29031
PageCount 15
ParticipantIDs doaj_primary_oai_doaj_org_article_25c8f8de5f1a4f48807c129340a06156
pubmedcentral_primary_oai_pubmedcentral_nih_gov_6238139
hal_primary_oai_HAL_hal_01926457v1
proquest_miscellaneous_2135120449
proquest_journals_2139122709
crossref_primary_10_15252_msb_20188516
pubmed_primary_30446599
wiley_primary_10_15252_msb_20188516_MSB188516
springer_journals_10_15252_msb_20188516
PublicationCentury 2000
PublicationDate November 2018
PublicationDateYYYYMMDD 2018-11-01
PublicationDate_xml – month: 11
  year: 2018
  text: November 2018
PublicationDecade 2010
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
– name: Hoboken
PublicationTitle Molecular systems biology
PublicationTitleAbbrev Mol Syst Biol
PublicationTitleAlternate Mol Syst Biol
PublicationYear 2018
Publisher Nature Publishing Group UK
EMBO Press
John Wiley and Sons Inc
Springer Nature
Publisher_xml – name: Nature Publishing Group UK
– name: EMBO Press
– name: John Wiley and Sons Inc
– name: Springer Nature
References Hwang, Vecchiarelli, Han, Mizuuchi, Harada, Funnell, Mizuuchi (CR32) 2013; 32
Graham, Wang, Song, Etson, van Oijen, Rudner, Loparo (CR27) 2014; 28
Rodionov, Lobocka, Yarmolinsky (CR49) 1999; 283
Parry, Surovtsev, Cabeen, O'Hern, Dufresne, Jacobs‐Wagner (CR46) 2014; 156
Broedersz, Wang, Meir, Loparo, Rudner, Wingreen (CR12) 2014; 111
Phillips, Kondev, Theriot, Garcia (CR47) 2012
Kumar, Mommer, Sourjik (CR33) 2010; 98
Funnell, Gagnier (CR23) 1993; 268
Lin, Grossman (CR38) 1998; 92
Bouet, Funnell (CR6) 1999; 18
Meyer, Grainger (CR41) 2013; 83
Gerdes, Moller‐Jensen, Bugge Jensen (CR26) 2000; 37
Das, Chattoraj (CR16) 2004; 54
Pillet, Sanchez, Lane, Anton Leberre, Bouet (CR48) 2011; 39
Vecchiarelli, Mizuuchi, Funnell (CR57) 2012; 86
Schiessel (CR901) 2013
Sanchez, Cattoni, Walter, Rech, Parmeggiani, Nollmann, Bouet (CR52) 2015; 1
Breier, Grossman (CR11) 2007; 64
Scholefield, Whiting, Errington, Murray (CR53) 2011; 79
Song, Rodrigues, Graham, Loparo (CR55) 2017; 45
CR4
Baek, Rajagopala, Chattoraj (CR3) 2014; 5
Saint‐Dic, Frushour, Kehrl, Kahng (CR50) 2006; 188
Hu, Vecchiarelli, Mizuuchi, Neuman, Liu (CR31) 2017; 112
Le Gall, Cattoni, Guilhas, Mathieu‐Demaziere, Oudjedi, Fiche, Rech, Abrahamsson, Murray, Bouet, Nollmann (CR35) 2016; 7
Taylor, Pastrana, Butterer, Pernstich, Gwynn, Sobott, Moreno‐Herrero, Dillingham (CR56) 2015; 43
Diaz, Rech, Bouet (CR18) 2015; 80
Diaz, Sanchez, Anton Le Berre, Bouet, Espéli (CR19) 2017
Murray, Ferreira, Errington (CR44) 2006; 61
de Gennes (CR25) 1979
Bouet, Lane (CR10) 2009; 284
Walter, Walliser, David, Dorignac, Geniet, Palmeri, Parmeggiani, Wingreen, Broedersz (CR59) 2018; 20
Bouet, Rech, Egloff, Biek, Lane (CR8) 2005; 55
Herring, Raffaelle, Allen, Kanin, Landick, Ansari, Palsson (CR30) 2005; 187
Fung, Bouet, Funnell (CR22) 2001; 20
Helsberg, Eichenlaub (CR29) 1986; 165
Castaing, Bouet, Lane (CR13) 2008; 70
Murray, Errington (CR45) 2008; 135
Sanchez, Rech, Gasc, Bouet (CR51) 2013; 41
Hanai, Liu, Benedetti, Caron, Lynch, Wang (CR28) 1996; 271
Schumacher, Tonthat, Lee, Rodriguez‐Castaneda, Chinnam, Kalliomaa‐Sanford, Ng, Barge, Shaw, Barilla (CR54) 2015; 349
Datsenko, Wanner (CR17) 2000; 97
Miller (CR42) 1972
Lim, Surovtsev, Beltran, Huang, Bewersdorf, Jacobs‐Wagner (CR37) 2014; 3
Collins, Pritchard (CR14) 1973; 78
Lemonnier, Bouet, Libante, Lane (CR36) 2000; 38
Lobocka, Yarmolinsky (CR39) 1996; 259
Mori, Kondo, Ohshima, Ogura, Hiraga (CR43) 1986; 192
Bouet, Ah‐Seng, Benmeradi, Lane (CR9) 2007; 63
Yamaichi, Niki (CR60) 2000; 97
Donczew, Mackiewicz, Wrobel, Flardh, Zakrzewska‐Czerwinska, Jakimowicz (CR20) 2016; 6
Ah‐Seng, Rech, Lane, Bouet (CR2) 2013; 9
Bouet, Surtees, Funnell (CR7) 2000; 275
Ah‐Seng, Lopez, Pasta, Lane, Bouet (CR1) 2009; 284
Cornet, Mortier, Patte, Louarn (CR15) 1994; 176
Fisher, Pastrana, Higman, Koh, Taylor, Butterer, Craggs, Sobott, Murray, Crump, Moreno‐Herrero, Dillingham (CR21) 2017; 6
Lynch, Wang (CR40) 1995; 92
Biek, Shi (CR5) 1994; 91
Funnell (CR24) 2016; 3
Lagage, Boccard, Vallet‐Gely (CR34) 2016; 12
Walter, Dorignac, Lorman, Rech, Bouet, Nollmann, Palmeri, Parmeggiani, Geniet (CR58) 2017; 119
2017; 119
2017; 6
1994; 176
2010; 98
2017; 45
1999; 283
1972
2015; 80
2015; 349
2014; 28
2017; 112
2008; 70
1979
2013; 9
2014; 5
2014; 3
2006; 61
2014; 2
2005; 187
1999; 18
2000; 97
2015; 43
1986; 192
1998; 92
2009; 284
2007; 63
2007; 64
1996; 259
2015; 1
1995; 92
2012
1973; 78
2013; 83
2013; 41
2011; 79
2000; 275
1993; 268
2011; 39
2014; 111
2018; 20
2001; 20
2016; 12
2014; 156
2004; 54
2016; 6
2016; 7
2000; 38
2016; 3
1986; 165
2000; 37
2013; 32
1996; 271
2017
2008; 135
2013
1994; 91
2005; 55
2006; 188
2012; 86
e_1_2_9_31_1
e_1_2_9_52_1
e_1_2_9_50_1
e_1_2_9_10_1
e_1_2_9_35_1
e_1_2_9_56_1
e_1_2_9_12_1
Gennes PG (e_1_2_9_26_1) 1979
e_1_2_9_33_1
e_1_2_9_54_1
e_1_2_9_14_1
e_1_2_9_39_1
e_1_2_9_16_1
e_1_2_9_37_1
e_1_2_9_58_1
e_1_2_9_18_1
e_1_2_9_41_1
e_1_2_9_20_1
e_1_2_9_62_1
e_1_2_9_22_1
e_1_2_9_45_1
e_1_2_9_8_1
Miller JH (e_1_2_9_43_1) 1972
e_1_2_9_6_1
e_1_2_9_4_1
e_1_2_9_60_1
e_1_2_9_2_1
e_1_2_9_49_1
e_1_2_9_28_1
e_1_2_9_47_1
e_1_2_9_30_1
e_1_2_9_53_1
e_1_2_9_51_1
e_1_2_9_11_1
e_1_2_9_34_1
e_1_2_9_57_1
e_1_2_9_13_1
e_1_2_9_32_1
e_1_2_9_55_1
e_1_2_9_15_1
e_1_2_9_38_1
e_1_2_9_17_1
e_1_2_9_36_1
e_1_2_9_59_1
e_1_2_9_19_1
e_1_2_9_42_1
e_1_2_9_40_1
e_1_2_9_61_1
e_1_2_9_21_1
e_1_2_9_46_1
e_1_2_9_23_1
e_1_2_9_44_1
e_1_2_9_7_1
e_1_2_9_5_1
e_1_2_9_3_1
e_1_2_9_9_1
e_1_2_9_25_1
e_1_2_9_27_1
e_1_2_9_48_1
Funnell BE (e_1_2_9_24_1) 1993; 268
e_1_2_9_29_1
References_xml – volume: 349
  start-page: 1120
  year: 2015
  end-page: 1124
  ident: CR54
  article-title: Structures of archaeal DNA segregation machinery reveal bacterial and eukaryotic linkages
  publication-title: Science
  contributor:
    fullname: Barilla
– volume: 63
  start-page: 468
  year: 2007
  end-page: 481
  ident: CR9
  article-title: Polymerization of SopA partition ATPase: regulation by DNA binding and SopB
  publication-title: Mol Microbiol
  contributor:
    fullname: Lane
– volume: 98
  start-page: 552
  year: 2010
  end-page: 559
  ident: CR33
  article-title: Mobility of cytoplasmic, membrane, and DNA‐binding proteins in
  publication-title: Biophys J
  contributor:
    fullname: Sourjik
– ident: CR4
– volume: 64
  start-page: 703
  year: 2007
  end-page: 718
  ident: CR11
  article-title: Whole‐genome analysis of the chromosome partitioning and sporulation protein Spo0J (ParB) reveals spreading and origin‐distal sites on the chromosome
  publication-title: Mol Microbiol
  contributor:
    fullname: Grossman
– volume: 83
  start-page: 69
  year: 2013
  end-page: 86
  ident: CR41
  article-title: The nucleoid in stationary phase
  publication-title: Adv Appl Microbiol
  contributor:
    fullname: Grainger
– volume: 61
  start-page: 1352
  year: 2006
  end-page: 1361
  ident: CR44
  article-title: The bacterial chromosome segregation protein Spo0J spreads along DNA from parS nucleation sites
  publication-title: Mol Microbiol
  contributor:
    fullname: Errington
– volume: 188
  start-page: 5626
  year: 2006
  end-page: 5631
  ident: CR50
  article-title: A parA homolog selectively influences positioning of the large chromosome origin in
  publication-title: J Bacteriol
  contributor:
    fullname: Kahng
– volume: 32
  start-page: 1238
  year: 2013
  end-page: 1249
  ident: CR32
  article-title: ParA‐mediated plasmid partition driven by protein pattern self‐organization
  publication-title: EMBO J
  contributor:
    fullname: Mizuuchi
– volume: 18
  start-page: 1415
  year: 1999
  end-page: 1424
  ident: CR6
  article-title: P1 ParA interacts with the P1 partition complex at and an ATP‐ADP switch controls ParA activities
  publication-title: EMBO J
  contributor:
    fullname: Funnell
– volume: 55
  start-page: 511
  year: 2005
  end-page: 525
  ident: CR8
  article-title: Probing plasmid partition with centromere‐based incompatibility
  publication-title: Mol Microbiol
  contributor:
    fullname: Lane
– year: 2012
  ident: CR47
  publication-title: Physical biology of the cell
  contributor:
    fullname: Garcia
– volume: 38
  start-page: 493
  year: 2000
  end-page: 505
  ident: CR36
  article-title: Disruption of the F plasmid partition complex by partition protein SopA
  publication-title: Mol Microbiol
  contributor:
    fullname: Lane
– volume: 37
  start-page: 455
  year: 2000
  end-page: 466
  ident: CR26
  article-title: Plasmid and chromosome partitioning: surprises from phylogeny
  publication-title: Mol Microbiol
  contributor:
    fullname: Bugge Jensen
– volume: 7
  start-page: 12107
  year: 2016
  ident: CR35
  article-title: Bacterial partition complexes segregate within the volume of the nucleoid
  publication-title: Nat Commun
  contributor:
    fullname: Nollmann
– volume: 92
  start-page: 675
  year: 1998
  end-page: 685
  ident: CR38
  article-title: Identification and characterization of a bacterial chromosome partitioning site
  publication-title: Cell
  contributor:
    fullname: Grossman
– volume: 70
  start-page: 1000
  year: 2008
  end-page: 1011
  ident: CR13
  article-title: F plasmid partition depends on interaction of SopA with non‐specific DNA
  publication-title: Mol Microbiol
  contributor:
    fullname: Lane
– volume: 97
  start-page: 14656
  year: 2000
  end-page: 14661
  ident: CR60
  article-title: Active segregation by the partitioning system in
  publication-title: Proc Natl Acad Sci USA
  contributor:
    fullname: Niki
– volume: 6
  start-page: 150263
  year: 2016
  ident: CR20
  article-title: ParA and ParB coordinate chromosome segregation with cell elongation and division during Streptomyces sporulation
  publication-title: Open Biol
  contributor:
    fullname: Jakimowicz
– volume: 176
  start-page: 3188
  year: 1994
  end-page: 3195
  ident: CR15
  article-title: Plasmid pSC101 harbors a recombination site, , which is able to resolve plasmid multimers and to substitute for the analogous chromosomal site
  publication-title: J Bacteriol
  contributor:
    fullname: Louarn
– volume: 112
  start-page: 1489
  year: 2017
  end-page: 1502
  ident: CR31
  article-title: Brownian Ratchet mechanism for faithful segregation of low‐copy‐number plasmids
  publication-title: Biophys J
  contributor:
    fullname: Liu
– volume: 259
  start-page: 366
  year: 1996
  end-page: 382
  ident: CR39
  article-title: P1 plasmid partition: a mutational analysis of ParB
  publication-title: J Mol Biol
  contributor:
    fullname: Yarmolinsky
– volume: 41
  start-page: 3094
  year: 2013
  end-page: 3103
  ident: CR51
  article-title: Insight into centromere‐binding properties of ParB proteins: a secondary binding motif is essential for bacterial genome maintenance
  publication-title: Nucleic Acids Res
  contributor:
    fullname: Bouet
– volume: 43
  start-page: 719
  year: 2015
  end-page: 731
  ident: CR56
  article-title: Specific and non‐specific interactions of ParB with DNA: implications for chromosome segregation
  publication-title: Nucleic Acids Res
  contributor:
    fullname: Dillingham
– start-page: 61
  year: 2017
  end-page: 73
  ident: CR19
  article-title: High‐resolution chromatin immunoprecipitation: ChIP‐sequencing
  publication-title: The bacterial nucleoid methods in molecular biology
  contributor:
    fullname: Espéli
– volume: 45
  start-page: 7106
  year: 2017
  end-page: 7117
  ident: CR55
  article-title: A network of cis and trans interactions is required for ParB spreading
  publication-title: Nucleic Acids Res
  contributor:
    fullname: Loparo
– volume: 20
  start-page: 035002
  year: 2018
  ident: CR59
  article-title: Looping and clustering model for the organization of protein‐DNA complexes on the bacterial genome
  publication-title: New J Phys
  contributor:
    fullname: Broedersz
– volume: 1
  start-page: 163
  year: 2015
  end-page: 173
  ident: CR52
  article-title: Stochastic self‐assembly of ParB proteins builds the bacterial DNA segregation apparatus
  publication-title: Cell Syst
  contributor:
    fullname: Bouet
– volume: 119
  start-page: 028101
  year: 2017
  ident: CR58
  article-title: Surfing on protein waves: proteophoresis as a mechanism for bacterial genome partitioning
  publication-title: Phys Rev Lett
  contributor:
    fullname: Geniet
– volume: 268
  start-page: 3616
  year: 1993
  end-page: 3624
  ident: CR23
  article-title: The P1 plasmid partition complex at parS: II. Analysis of ParB protein binding activity and specificity
  publication-title: J Biol Chem
  contributor:
    fullname: Gagnier
– volume: 12
  start-page: e1006428
  year: 2016
  ident: CR34
  article-title: Regional control of chromosome segregation in
  publication-title: PLoS Genet
  contributor:
    fullname: Vallet‐Gely
– volume: 20
  start-page: 4901
  year: 2001
  end-page: 4911
  ident: CR22
  article-title: Probing the ATP‐binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis
  publication-title: EMBO J
  contributor:
    fullname: Funnell
– volume: 3
  start-page: 44
  year: 2016
  ident: CR24
  article-title: ParB partition proteins: complex formation and spreading at bacterial and plasmid centromeres
  publication-title: Front Mol Biosci
  contributor:
    fullname: Funnell
– volume: 165
  start-page: 1043
  year: 1986
  end-page: 1045
  ident: CR29
  article-title: Twelve 43‐base‐pair repeats map in a ‐acting region essential for partition of plasmid mini‐F
  publication-title: J Bacteriol
  contributor:
    fullname: Eichenlaub
– volume: 78
  start-page: 143
  year: 1973
  end-page: 155
  ident: CR14
  article-title: Relationship between chromosome replication and F'lac episome replication in
  publication-title: J Mol Biol
  contributor:
    fullname: Pritchard
– volume: 54
  start-page: 836
  year: 2004
  end-page: 849
  ident: CR16
  article-title: Origin pairing (‘handcuffing’) and unpairing in the control of P1 plasmid replication
  publication-title: Mol Microbiol
  contributor:
    fullname: Chattoraj
– volume: 79
  start-page: 1089
  year: 2011
  end-page: 1100
  ident: CR53
  article-title: Spo0J regulates the oligomeric state of Soj to trigger its switch from an activator to an inhibitor of DNA replication initiation
  publication-title: Mol Microbiol
  contributor:
    fullname: Murray
– volume: 284
  start-page: 165
  year: 2009
  end-page: 173
  ident: CR10
  article-title: Molecular basis of the supercoil deficit induced by the mini‐F plasmid partition complex
  publication-title: J Biol Chem
  contributor:
    fullname: Lane
– volume: 28
  start-page: 1228
  year: 2014
  end-page: 1238
  ident: CR27
  article-title: ParB spreading requires DNA bridging
  publication-title: Genes Dev
  contributor:
    fullname: Loparo
– volume: 97
  start-page: 6640
  year: 2000
  end-page: 6645
  ident: CR17
  article-title: One‐step inactivation of chromosomal genes in K‐12 using PCR products
  publication-title: Proc Natl Acad Sci USA
  contributor:
    fullname: Wanner
– volume: 283
  start-page: 546
  year: 1999
  end-page: 549
  ident: CR49
  article-title: Silencing of genes flanking the P1 plasmid centromere
  publication-title: Science
  contributor:
    fullname: Yarmolinsky
– volume: 80
  start-page: 54
  year: 2015
  end-page: 62
  ident: CR18
  article-title: Imaging centromere‐based incompatibilities: insights into the mechanism of incompatibility mediated by low‐copy number plasmids
  publication-title: Plasmid
  contributor:
    fullname: Bouet
– volume: 39
  start-page: 7477
  year: 2011
  end-page: 7486
  ident: CR48
  article-title: Centromere binding specificity in assembly of the F plasmid partition complex
  publication-title: Nucleic Acids Res
  contributor:
    fullname: Bouet
– volume: 9
  start-page: e1003956
  year: 2013
  ident: CR2
  article-title: Defining the role of ATP hydrolysis in mitotic segregation of bacterial plasmids
  publication-title: PLoS Genet
  contributor:
    fullname: Bouet
– volume: 135
  start-page: 74
  year: 2008
  end-page: 84
  ident: CR45
  article-title: Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA
  publication-title: Cell
  contributor:
    fullname: Errington
– volume: 91
  start-page: 8027
  year: 1994
  end-page: 8031
  ident: CR5
  article-title: A single 43‐bp sopC repeat of plasmid mini‐F is sufficient to allow assembly of a functional nucleoprotein partition complex
  publication-title: Proc Natl Acad Sci USA
  contributor:
    fullname: Shi
– year: 1979
  ident: CR25
  publication-title: Scaling concept in polymer physics
  contributor:
    fullname: de Gennes
– volume: 156
  start-page: 183
  year: 2014
  end-page: 194
  ident: CR46
  article-title: The bacterial cytoplasm has glass‐like properties and is fluidized by metabolic activity
  publication-title: Cell
  contributor:
    fullname: Jacobs‐Wagner
– volume: 192
  start-page: 1
  year: 1986
  end-page: 15
  ident: CR43
  article-title: Structure and function of the F plasmid genes essential for partitioning
  publication-title: J Mol Biol
  contributor:
    fullname: Hiraga
– year: 2013
  ident: CR901
  publication-title: Biophysics for beginners: a journey through the cell nucleus
  contributor:
    fullname: Schiessel
– volume: 275
  start-page: 8213
  year: 2000
  end-page: 8219
  ident: CR7
  article-title: Stoichiometry of P1 plasmid partition complexes
  publication-title: J Biol Chem
  contributor:
    fullname: Funnell
– volume: 111
  start-page: 8809
  year: 2014
  end-page: 8814
  ident: CR12
  article-title: Condensation and localization of the partitioning protein ParB on the bacterial chromosome
  publication-title: Proc Natl Acad Sci USA
  contributor:
    fullname: Wingreen
– year: 1972
  ident: CR42
  publication-title: Experiments in molecular genetics
  contributor:
    fullname: Miller
– volume: 3
  start-page: e02758
  year: 2014
  ident: CR37
  article-title: Evidence for a DNA‐relay mechanism in ParABS‐mediated chromosome segregation
  publication-title: eLife
  contributor:
    fullname: Jacobs‐Wagner
– volume: 284
  start-page: 30067
  year: 2009
  end-page: 30075
  ident: CR1
  article-title: Dual role of DNA in regulating ATP hydrolysis by the SopA partition protein
  publication-title: J Biol Chem
  contributor:
    fullname: Bouet
– volume: 92
  start-page: 1896
  year: 1995
  end-page: 1900
  ident: CR40
  article-title: SopB protein‐meditated silencing of genes linked to the locus of F plasmid
  publication-title: Proc Natl Acad Sci USA
  contributor:
    fullname: Wang
– volume: 271
  start-page: 17469
  year: 1996
  end-page: 17475
  ident: CR28
  article-title: Molecular dissection of a protein SopB essential for F plasmid partition
  publication-title: J Biol Chem
  contributor:
    fullname: Wang
– volume: 6
  start-page: e28086
  year: 2017
  ident: CR21
  article-title: The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere
  publication-title: eLife
  contributor:
    fullname: Dillingham
– volume: 5
  start-page: e01061–01014
  year: 2014
  ident: CR3
  article-title: Chromosome segregation proteins of as transcription regulators
  publication-title: MBio
  contributor:
    fullname: Chattoraj
– volume: 187
  start-page: 6166
  year: 2005
  end-page: 6174
  ident: CR30
  article-title: Immobilization of RNA polymerase and location of binding sites by use of chromatin immunoprecipitation and microarrays
  publication-title: J Bacteriol
  contributor:
    fullname: Palsson
– volume: 86
  start-page: 513
  year: 2012
  end-page: 523
  ident: CR57
  article-title: Surfing biological surfaces: exploiting the nucleoid for partition and transport in bacteria
  publication-title: Mol Microbiol
  contributor:
    fullname: Funnell
– volume: 176
  start-page: 3188
  year: 1994
  end-page: 3195
  article-title: Plasmid pSC101 harbors a recombination site, , which is able to resolve plasmid multimers and to substitute for the analogous chromosomal site
  publication-title: J Bacteriol
– volume: 18
  start-page: 1415
  year: 1999
  end-page: 1424
  article-title: P1 ParA interacts with the P1 partition complex at and an ATP‐ADP switch controls ParA activities
  publication-title: EMBO J
– volume: 45
  start-page: 7106
  year: 2017
  end-page: 7117
  article-title: A network of cis and trans interactions is required for ParB spreading
  publication-title: Nucleic Acids Res
– volume: 112
  start-page: 1489
  year: 2017
  end-page: 1502
  article-title: Brownian Ratchet mechanism for faithful segregation of low‐copy‐number plasmids
  publication-title: Biophys J
– volume: 259
  start-page: 366
  year: 1996
  end-page: 382
  article-title: P1 plasmid partition: a mutational analysis of ParB
  publication-title: J Mol Biol
– volume: 37
  start-page: 455
  year: 2000
  end-page: 466
  article-title: Plasmid and chromosome partitioning: surprises from phylogeny
  publication-title: Mol Microbiol
– volume: 283
  start-page: 546
  year: 1999
  end-page: 549
  article-title: Silencing of genes flanking the P1 plasmid centromere
  publication-title: Science
– volume: 78
  start-page: 143
  year: 1973
  end-page: 155
  article-title: Relationship between chromosome replication and F'lac episome replication in
  publication-title: J Mol Biol
– volume: 3
  start-page: e02758
  year: 2014
  article-title: Evidence for a DNA‐relay mechanism in ParABS‐mediated chromosome segregation
  publication-title: eLife
– year: 1979
– volume: 268
  start-page: 3616
  year: 1993
  end-page: 3624
  article-title: The P1 plasmid partition complex at parS: II. Analysis of ParB protein binding activity and specificity
  publication-title: J Biol Chem
– volume: 5
  start-page: e01061–01014
  year: 2014
  article-title: Chromosome segregation proteins of as transcription regulators
  publication-title: MBio
– volume: 55
  start-page: 511
  year: 2005
  end-page: 525
  article-title: Probing plasmid partition with centromere‐based incompatibility
  publication-title: Mol Microbiol
– volume: 61
  start-page: 1352
  year: 2006
  end-page: 1361
  article-title: The bacterial chromosome segregation protein Spo0J spreads along DNA from parS nucleation sites
  publication-title: Mol Microbiol
– volume: 9
  start-page: e1003956
  year: 2013
  article-title: Defining the role of ATP hydrolysis in mitotic segregation of bacterial plasmids
  publication-title: PLoS Genet
– volume: 63
  start-page: 468
  year: 2007
  end-page: 481
  article-title: Polymerization of SopA partition ATPase: regulation by DNA binding and SopB
  publication-title: Mol Microbiol
– volume: 6
  start-page: e28086
  year: 2017
  article-title: The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere
  publication-title: eLife
– volume: 38
  start-page: 493
  year: 2000
  end-page: 505
  article-title: Disruption of the F plasmid partition complex by partition protein SopA
  publication-title: Mol Microbiol
– volume: 83
  start-page: 69
  year: 2013
  end-page: 86
  article-title: The nucleoid in stationary phase
  publication-title: Adv Appl Microbiol
– volume: 80
  start-page: 54
  year: 2015
  end-page: 62
  article-title: Imaging centromere‐based incompatibilities: insights into the mechanism of incompatibility mediated by low‐copy number plasmids
  publication-title: Plasmid
– volume: 32
  start-page: 1238
  year: 2013
  end-page: 1249
  article-title: ParA‐mediated plasmid partition driven by protein pattern self‐organization
  publication-title: EMBO J
– volume: 3
  start-page: 44
  year: 2016
  article-title: ParB partition proteins: complex formation and spreading at bacterial and plasmid centromeres
  publication-title: Front Mol Biosci
– year: 1972
– volume: 92
  start-page: 1896
  year: 1995
  end-page: 1900
  article-title: SopB protein‐meditated silencing of genes linked to the locus of F plasmid
  publication-title: Proc Natl Acad Sci USA
– volume: 28
  start-page: 1228
  year: 2014
  end-page: 1238
  article-title: ParB spreading requires DNA bridging
  publication-title: Genes Dev
– volume: 43
  start-page: 719
  year: 2015
  end-page: 731
  article-title: Specific and non‐specific interactions of ParB with DNA: implications for chromosome segregation
  publication-title: Nucleic Acids Res
– volume: 92
  start-page: 675
  year: 1998
  end-page: 685
  article-title: Identification and characterization of a bacterial chromosome partitioning site
  publication-title: Cell
– volume: 79
  start-page: 1089
  year: 2011
  end-page: 1100
  article-title: Spo0J regulates the oligomeric state of Soj to trigger its switch from an activator to an inhibitor of DNA replication initiation
  publication-title: Mol Microbiol
– volume: 156
  start-page: 183
  year: 2014
  end-page: 194
  article-title: The bacterial cytoplasm has glass‐like properties and is fluidized by metabolic activity
  publication-title: Cell
– volume: 97
  start-page: 14656
  year: 2000
  end-page: 14661
  article-title: Active segregation by the partitioning system in
  publication-title: Proc Natl Acad Sci USA
– volume: 97
  start-page: 6640
  year: 2000
  end-page: 6645
  article-title: One‐step inactivation of chromosomal genes in K‐12 using PCR products
  publication-title: Proc Natl Acad Sci USA
– volume: 349
  start-page: 1120
  year: 2015
  end-page: 1124
  article-title: Structures of archaeal DNA segregation machinery reveal bacterial and eukaryotic linkages
  publication-title: Science
– volume: 275
  start-page: 8213
  year: 2000
  end-page: 8219
  article-title: Stoichiometry of P1 plasmid partition complexes
  publication-title: J Biol Chem
– volume: 119
  start-page: 028101
  year: 2017
  article-title: Surfing on protein waves: proteophoresis as a mechanism for bacterial genome partitioning
  publication-title: Phys Rev Lett
– volume: 2
  year: 2014
  article-title: Plasmid partition mechanisms
  publication-title: Microbiol Spectr
– volume: 165
  start-page: 1043
  year: 1986
  end-page: 1045
  article-title: Twelve 43‐base‐pair repeats map in a ‐acting region essential for partition of plasmid mini‐F
  publication-title: J Bacteriol
– start-page: 61
  year: 2017
  end-page: 73
– volume: 284
  start-page: 30067
  year: 2009
  end-page: 30075
  article-title: Dual role of DNA in regulating ATP hydrolysis by the SopA partition protein
  publication-title: J Biol Chem
– volume: 188
  start-page: 5626
  year: 2006
  end-page: 5631
  article-title: A parA homolog selectively influences positioning of the large chromosome origin in
  publication-title: J Bacteriol
– volume: 20
  start-page: 4901
  year: 2001
  end-page: 4911
  article-title: Probing the ATP‐binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis
  publication-title: EMBO J
– year: 2012
– volume: 271
  start-page: 17469
  year: 1996
  end-page: 17475
  article-title: Molecular dissection of a protein SopB essential for F plasmid partition
  publication-title: J Biol Chem
– volume: 284
  start-page: 165
  year: 2009
  end-page: 173
  article-title: Molecular basis of the supercoil deficit induced by the mini‐F plasmid partition complex
  publication-title: J Biol Chem
– volume: 192
  start-page: 1
  year: 1986
  end-page: 15
  article-title: Structure and function of the F plasmid genes essential for partitioning
  publication-title: J Mol Biol
– volume: 39
  start-page: 7477
  year: 2011
  end-page: 7486
  article-title: Centromere binding specificity in assembly of the F plasmid partition complex
  publication-title: Nucleic Acids Res
– volume: 1
  start-page: 163
  year: 2015
  end-page: 173
  article-title: Stochastic self‐assembly of ParB proteins builds the bacterial DNA segregation apparatus
  publication-title: Cell Syst
– volume: 91
  start-page: 8027
  year: 1994
  end-page: 8031
  article-title: A single 43‐bp sopC repeat of plasmid mini‐F is sufficient to allow assembly of a functional nucleoprotein partition complex
  publication-title: Proc Natl Acad Sci USA
– volume: 7
  start-page: 12107
  year: 2016
  article-title: Bacterial partition complexes segregate within the volume of the nucleoid
  publication-title: Nat Commun
– volume: 86
  start-page: 513
  year: 2012
  end-page: 523
  article-title: Surfing biological surfaces: exploiting the nucleoid for partition and transport in bacteria
  publication-title: Mol Microbiol
– volume: 111
  start-page: 8809
  year: 2014
  end-page: 8814
  article-title: Condensation and localization of the partitioning protein ParB on the bacterial chromosome
  publication-title: Proc Natl Acad Sci USA
– volume: 70
  start-page: 1000
  year: 2008
  end-page: 1011
  article-title: F plasmid partition depends on interaction of SopA with non‐specific DNA
  publication-title: Mol Microbiol
– volume: 64
  start-page: 703
  year: 2007
  end-page: 718
  article-title: Whole‐genome analysis of the chromosome partitioning and sporulation protein Spo0J (ParB) reveals spreading and origin‐distal sites on the chromosome
  publication-title: Mol Microbiol
– volume: 98
  start-page: 552
  year: 2010
  end-page: 559
  article-title: Mobility of cytoplasmic, membrane, and DNA‐binding proteins in
  publication-title: Biophys J
– volume: 12
  start-page: e1006428
  year: 2016
  article-title: Regional control of chromosome segregation in
  publication-title: PLoS Genet
– volume: 41
  start-page: 3094
  year: 2013
  end-page: 3103
  article-title: Insight into centromere‐binding properties of ParB proteins: a secondary binding motif is essential for bacterial genome maintenance
  publication-title: Nucleic Acids Res
– volume: 54
  start-page: 836
  year: 2004
  end-page: 849
  article-title: Origin pairing (‘handcuffing’) and unpairing in the control of P1 plasmid replication
  publication-title: Mol Microbiol
– volume: 135
  start-page: 74
  year: 2008
  end-page: 84
  article-title: Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA
  publication-title: Cell
– volume: 6
  start-page: 150263
  year: 2016
  article-title: ParA and ParB coordinate chromosome segregation with cell elongation and division during Streptomyces sporulation
  publication-title: Open Biol
– volume: 20
  start-page: 035002
  year: 2018
  article-title: Looping and clustering model for the organization of protein‐DNA complexes on the bacterial genome
  publication-title: New J Phys
– volume: 187
  start-page: 6166
  year: 2005
  end-page: 6174
  article-title: Immobilization of RNA polymerase and location of binding sites by use of chromatin immunoprecipitation and microarrays
  publication-title: J Bacteriol
– year: 2013
– ident: e_1_2_9_42_1
  doi: 10.1016/B978-0-12-407678-5.00002-7
– ident: e_1_2_9_10_1
  doi: 10.1111/j.1365-2958.2006.05537.x
– ident: e_1_2_9_48_1
  doi: 10.1201/9781134111589
– ident: e_1_2_9_16_1
  doi: 10.1128/jb.176.11.3188-3195.1994
– ident: e_1_2_9_18_1
  doi: 10.1073/pnas.120163297
– ident: e_1_2_9_41_1
  doi: 10.1073/pnas.92.6.1896
– ident: e_1_2_9_9_1
  doi: 10.1111/j.1365-2958.2004.04396.x
– ident: e_1_2_9_2_1
  doi: 10.1074/jbc.M109.044800
– ident: e_1_2_9_51_1
  doi: 10.1128/JB.00250-06
– ident: e_1_2_9_4_1
  doi: 10.1128/mBio.01061-14
– ident: e_1_2_9_13_1
  doi: 10.1073/pnas.1402529111
– ident: e_1_2_9_8_1
  doi: 10.1074/jbc.275.11.8213
– volume-title: Scaling concept in polymer physics
  year: 1979
  ident: e_1_2_9_26_1
  contributor:
    fullname: Gennes PG
– ident: e_1_2_9_37_1
  doi: 10.1046/j.1365-2958.2000.02101.x
– ident: e_1_2_9_57_1
  doi: 10.1093/nar/gkx271
– ident: e_1_2_9_61_1
  doi: 10.1088/1367-2630/aaad39
– ident: e_1_2_9_6_1
  doi: 10.1073/pnas.91.17.8027
– volume-title: Experiments in molecular genetics
  year: 1972
  ident: e_1_2_9_43_1
  contributor:
    fullname: Miller JH
– ident: e_1_2_9_54_1
  doi: 10.1201/b16269
– ident: e_1_2_9_30_1
  doi: 10.1128/jb.165.3.1043-1045.1986
– ident: e_1_2_9_28_1
  doi: 10.1101/gad.242206.114
– ident: e_1_2_9_7_1
  doi: 10.1093/emboj/18.5.1415
– ident: e_1_2_9_44_1
  doi: 10.1016/0022-2836(86)90459-6
– ident: e_1_2_9_59_1
  doi: 10.1111/mmi.12017
– ident: e_1_2_9_60_1
  doi: 10.1103/PhysRevLett.119.028101
– ident: e_1_2_9_36_1
  doi: 10.1038/ncomms12107
– ident: e_1_2_9_58_1
  doi: 10.1093/nar/gku1295
– ident: e_1_2_9_32_1
  doi: 10.1016/j.bpj.2017.02.039
– ident: e_1_2_9_35_1
  doi: 10.1371/journal.pgen.1006428
– ident: e_1_2_9_47_1
  doi: 10.1016/j.cell.2013.11.028
– ident: e_1_2_9_53_1
  doi: 10.1016/j.cels.2015.07.013
– ident: e_1_2_9_3_1
  doi: 10.1371/journal.pgen.1003956
– ident: e_1_2_9_29_1
  doi: 10.1074/jbc.271.29.17469
– ident: e_1_2_9_27_1
  doi: 10.1046/j.1365-2958.2000.01975.x
– ident: e_1_2_9_34_1
  doi: 10.1016/j.bpj.2009.11.002
– ident: e_1_2_9_56_1
  doi: 10.1126/science.aaa9046
– ident: e_1_2_9_46_1
  doi: 10.1016/j.cell.2008.07.044
– ident: e_1_2_9_33_1
  doi: 10.1038/emboj.2013.34
– ident: e_1_2_9_31_1
  doi: 10.1128/JB.187.17.6166-6174.2005
– volume: 268
  start-page: 3616
  year: 1993
  ident: e_1_2_9_24_1
  article-title: The P1 plasmid partition complex at parS: II. Analysis of ParB protein binding activity and specificity
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(18)53738-8
  contributor:
    fullname: Funnell BE
– ident: e_1_2_9_55_1
  doi: 10.1111/j.1365-2958.2010.07507.x
– ident: e_1_2_9_14_1
  doi: 10.1111/j.1365-2958.2008.06465.x
– ident: e_1_2_9_20_1
  doi: 10.1007/978-1-4939-7098-8_6
– ident: e_1_2_9_25_1
  doi: 10.3389/fmolb.2016.00044
– ident: e_1_2_9_45_1
  doi: 10.1111/j.1365-2958.2006.05316.x
– ident: e_1_2_9_50_1
  doi: 10.1126/science.283.5401.546
– ident: e_1_2_9_11_1
  doi: 10.1074/jbc.M802752200
– ident: e_1_2_9_38_1
  doi: 10.7554/eLife.02758
– ident: e_1_2_9_22_1
  doi: 10.7554/eLife.28086
– ident: e_1_2_9_21_1
  doi: 10.1098/rsob.150263
– ident: e_1_2_9_40_1
  doi: 10.1006/jmbi.1996.0326
– ident: e_1_2_9_17_1
  doi: 10.1111/j.1365-2958.2004.04322.x
– ident: e_1_2_9_39_1
  doi: 10.1016/S0092-8674(00)81135-6
– ident: e_1_2_9_12_1
  doi: 10.1111/j.1365-2958.2007.05690.x
– ident: e_1_2_9_49_1
  doi: 10.1093/nar/gkr457
– ident: e_1_2_9_62_1
  doi: 10.1073/pnas.97.26.14656
– ident: e_1_2_9_15_1
  doi: 10.1016/0022-2836(73)90434-8
– ident: e_1_2_9_5_1
  doi: 10.1128/microbiolspec.PLAS-0023-2014
– ident: e_1_2_9_52_1
  doi: 10.1093/nar/gkt018
– ident: e_1_2_9_23_1
  doi: 10.1093/emboj/20.17.4901
– ident: e_1_2_9_19_1
  doi: 10.1016/j.plasmid.2015.03.007
SSID ssj0038182
Score 2.5052633
Snippet Chromosome and plasmid segregation in bacteria are mostly driven by ParAB S systems. These DNA partitioning machineries rely on large nucleoprotein complexes...
Chromosome and plasmid segregation in bacteria are mostly driven by ParABS systems. These DNA partitioning machineries rely on large nucleoprotein complexes...
Chromosome and plasmid segregation in bacteria are mostly driven by ParAB systems. These DNA partitioning machineries rely on large nucleoprotein complexes...
Chromosome and plasmid segregation in bacteria are mostly driven by ParAB S systems. These DNA partitioning machineries rely on large nucleoprotein complexes...
Abstract Chromosome and plasmid segregation in bacteria are mostly driven by ParABS systems. These DNA partitioning machineries rely on large nucleoprotein...
SourceID doaj
pubmedcentral
hal
proquest
crossref
pubmed
wiley
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage e8516
SubjectTerms Adenosine triphosphatase
Assembly
Bacteria
Bacterial Proteins - metabolism
Bacteriology
Binding
Biochemistry, Molecular Biology
Biological Physics
Chromosome Segregation
Chromosomes
Chromosomes, Bacterial - genetics
Chromosomes, Bacterial - physiology
Coding
Deoxyribonucleic acid
DNA
DNA segregation
E coli
EMBO13
EMBO23
EMBO33
Escherichia coli
F plasmid
Life Sciences
Mathematical models
Microbiology and Parasitology
Models, Theoretical
Nucleation
ParABS
Partitions
Physics
plasmid partition
Plasmids
Plasmids - genetics
Plasmids - physiology
Proteins
Robustness (mathematics)
Stochastic Processes
Stochasticity
Systems Biology - methods
Transcription
Vibrio cholerae - metabolism
Vibrio cholerae - physiology
Waterborne diseases
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZQpUpcELQ8AgUZhOAU1fHaTnzcIqoVolygUi_IcvzQrkSyq01b0X_PTJwsRBX0wi3yK87MOPONPP5MyFvHo9ZBwUorIDYRPtZ5LZjPLSvrmdelKzweFD77ohbn4tOFvPjjqi_MCUv0wElwx1y6KlY-yFhYEdHcoD_4KMEseuNEts30GEylfzC6IT4wakou-XHT1ZjGVQG-UBMP1BP1g19ZYhrkbYx5O1Vyt186RbO9Ozp9SB4MOJLO0_wfkXuhPSD76WbJm0PyfU4d5klvr4OnTcDjvauuoX6LLLN0g5-NGqF9Rnn4SQFCh6b-cUOhrE4EzjC6W2KyXrduoI9tPd0A1G5WvntMzk8_fvuwyIebFHKneKlyXzERECwEBf82zSLzQcNKtcpJWdlZdBDVQSRUehBc5bWMFuK0utKiYMEC4npC9tp1G54RKrSvopNRReaEC4V2XNS2CEhlp3gIGXk3StdsEmGGwUAD1WBADWZUQ0ZOUPa7Rshz3ReA9s2gfXOX9jPyBjQ3GWMx_2ywDLGrErK8LjJyNCrWDCu0Mxygb8F5yXRGXu-qYW3hholtw_qqbwN4iAkBbZ4mO9i9aoY74VJDTTmxkMlcpjXtatnzdyuESTPo-X60pd_T-ouo8t7U_i1Qc_b1JD09_x-ifUHu48jp3OUR2bvcXoWXAMAu61f9WvsFMhwqBg
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Health & Medical Collection
  dbid: 7X7
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELagCIkL4s3SggxCcIrqeG0nPqEtolohygUq7QVZjh_sSiRZNm3V_ntm8qqiit4ivzMP-xt7PCbkveNR66BA01KwTYSPRVII5hPLsmLudeZSjxeFT76r5an4upKrfsOt6d0qhzmxnah97XCP_JADVEk5z5j-tP2b4KtReLraP6Fxl9yDrhS6dGWr0eDCxYj3cTUll_ywbAp05soBZajJOtSG64fVZY3OkDeR5k2HyfHUdIpp20Xp-BF52KNJuujY_5jcCdUTcr97X_LqKfm1oA69pXcXwdMy4CXfTVNSv8NYs3SLUoN8oa1febikAKRDWfy5opBWdGGcoXW3Rpe9pi6hjq083QLgLje-eUZOj7_8_LxM-vcUEqd4phKfMxEQMgQFM5xmkfmgQV-tclLmdh4d2HZgD2UeCJd7LaMFa63ItUhZsIC7npO9qq7CS0KF9nl0MqrInHAh1Y6LwqYBA9opHsKMfBioa7Zd2AyD5gaywQAbzMCGGTlC2o-FMNp1m1DvfpteeQyXLo-5DzKmVkScckCGAKcIZhGRQSPvgHOTNpaLbwbTEMEqIbOLdEYOBsaaXk8bcy1VM_J2zAYNw2MTW4X6vC0DqIgJAWVedHIwdjXH83CpISebSMhkLNOcarNuo3grBEtzqPlxkKXrYf2HVEkrarcT1Jz8OOq-Xt3-w_vkAdbp7lUekL2z3Xl4DQDrrHjTatE_rEUieg
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access(OpenAccess)
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1bi9QwFA66Ivgi6310lSiiT9U0k6bNg8isuAzi-qID-yIhzcUZ2HbGdnfZ-fd7Tm9LGRXfSm4N55J8h5x8IeS15UEpL8HTYohNhAt5lAvmIsPSfOpUamOHF4WPv8n5Qnw5SU6uKYU6AdZ_DO3wPalFdfru8vf2Izj8h-71Hv6-qHNM0soAPcib5BYXEKRjFp8YDhRwX-IdxeZOl9GW1DD3w0azxLzIXdC5mzs5HKCO4W2zPx3tk7sdsKSz1hLukRu-vE9ut09Nbh-QnzNqMXG6uvCOFh7v-67qgroKaWfpBg0IVUSbFHN_SQFT-yI_3VIoy1tGZxjdLjF7r14X0MeUjm4AexcrVz8ki6PPPz7No-5phchKnsrIZUx4RA9ewmKnWGDOK3BdI22SZGYaLIR5EBqlDgSXOZUEA4FbnikRM28Agj0ie-W69E8IFcplwSZBBmaF9bGyXOQm9shtJ7n3E_Kml67etAwaGiMPVIMGNeheDRNyiLIfGiHxdVOwrn7pzo80T2wWMueTEBsRcPUBcwLIIphBcAaDvALNjcaYz75qLEMwK0WSXsQTctArVvcWpzlg4ZjzlKkJeTlUg7PhCYop_fq8aQMAiQkBbR63djD8aopH44mCmnRkIaO5jGvK1bIh9JaIm6bQ821vS9fT-ouoosbU_i1Qffz9sP16-t8jPyN38LO9bXlA9s6qc_8cYNdZ_qJxqCs6rShp
  priority: 102
  providerName: Scholars Portal
– databaseName: SpringerOpen
  dbid: C6C
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3daxQxEA9aEXwRvz1bJYro02I2l2Q3j9fDcoj1RQt9kZBP7qC7d9y2xf73ndmP0-VQfFvytWE-Mr9hJhNC3nuetI4KNC0H30SE5DInWMgsK9w06MLnAS8Kn35TizPx5Vye90k0eBfmz_i95JJ_qhqHCVglIAN1l9wD81ti5tZczYcDF20O78tn7k0ZmZu2Kj8YkSXmPO4Dyv28yF1wdAxdW9tz8og87EEjnXVcfkzuxPoJud89I3nzlPycUY9J0dvrGGgV8S7vqqlo2GJJWbpB4UDy0zZ9PP6igJdj5S5uKLS5rlozrO6XmJnXrCuYY-tAN4Crq1VonpGzk88_5ousfzYh84oXKgslExGRQVRwkGmWWIga1NIqL2Vpp8mDCwduTxGAcGXQMllwylypRc6iBXj1nBzU6zq-JFToUCYvk0rMCx9z7blwNo9Yt07xGCfkw0Bds-mqYxj0KpANBthgBjZMyDHSfjcIi1q3DcBr0-uI4dKXqQxRptyKhCcLiArAEcEsAi9Y5B1wbrTGYvbVYBsCVSVkcZ1PyNHAWNOrY2M44Nyc84LpCXm76wZFwuiIreP6qh0D4IcJAWNedHKw-9UUw95SQ08xkpDRXsY99WrZFutWiImmMPPjIEu_t_UXUmWtqP2boOb0-3H39eq_Vz4kD_Czu0l5RA4ut1fxNUCqS_emVahbYYYZ6w
  priority: 102
  providerName: Springer Nature
– databaseName: Wiley Online Library (Open Access Collection)
  dbid: 24P
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3daxQxEA9aEXwRvz1bJYro02I2l2Q3j1exHGJF0EJfJOTTO3D3jtu22P--M_ulS1HwbcnXLpmZ5JfNzG8Iee150joqsLQcziYiJJc5wUJmWeHmQRc-DxgofPxZLU_Ex1N52uc5xViYjh9i_OGGltGu12jg1jVDxh5kDa0ah65ZJWAGdZPcQtYYJM_n4suwFONuxLuISJFhXqaeZBMHePdn98mm1HL3w1azQs_I67DzuvfkeIU6BbjtDnV0j9ztoSVddLpwn9yI9QNyu0s2efmQfF9Qj67Tu4sYaBUx4nfdVDTskHiWblGFUEi0dTKPvyig6li5n5cUylzH6Qyj-xX67zWbCvrYOtAtoO9qHZpH5OTow7f3y6xPrpB5xQuVhZKJiPghKljuNEssRA3Ga5WXsrTz5OGgB4ejIsAklkHLZOHo5kotchYtgLDHZK_e1PEpoUKHMnmZVGJe-Jhrz4WzeUR2O8VjnJE3w-yabcehYfDsgWIwIAYziGFGDnHux0ZIfd0WbHY_TG9JhktfpjJEmXIrEq4_oFAAWgSzCM9gkFcguckYy8Ung2UIZ5WQxUU-IweDYE1vtI3hgIZzzgumZ-TlWA3mhncoto6b87YNQCQmBLR50unB-Ko5Xo5LDTXFREMm3zKtqderltJbIXKaQ8-3gy79_qy_TFXWqtq_J9Qcfz3snp79Z_t9cgcLu6jLA7J3tjuPzwF-nbkXrYldAYszJnI
  priority: 102
  providerName: Wiley-Blackwell
Title A conserved mechanism drives partition complex assembly on bacterial chromosomes and plasmids
URI https://link.springer.com/article/10.15252/msb.20188516
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fmsb.20188516
https://www.ncbi.nlm.nih.gov/pubmed/30446599
https://www.proquest.com/docview/2139122709
https://search.proquest.com/docview/2135120449
https://hal.science/hal-01926457
https://pubmed.ncbi.nlm.nih.gov/PMC6238139
https://doaj.org/article/25c8f8de5f1a4f48807c129340a06156
Volume 14
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwED9tQ0i8IL4JjCogBE9ZE9d24se22lQhOlXApL6gKPEHrbSkVbtN7L_nzkk6VRM88BKljus6vt_5flefzwAfNXNKWYmalqBvwo0ro5LHJiritBwYlerE0Ebh6bmcXPAvczE_ANHthfFB-7pcntSX1Um9XPjYynWl-12cWH82HUuyMwPVP4RDBGjnojfTL1kg1ibTFEywfrUtKYIrQ2pB5xUNaAVT-FSvd3bIp-tH67KgYMj7TPN-wORu1XSf03qjdPYEHrdsMhw2vX4KB7Z-Bg-b8yVvn8PPYagpWnpzY01YWdrku9xWodlQrtlwTS9Lcgl9XLn9HSKRtlV5eRtiWdmkccbW9YJC9rarCr9T1CZcI-Gulmb7Ai7OTn-MJ1F7nkKkJUtlZLKYW6IMVuIMp2IXG6tQXwuphciKgdPo26E_lBocw8wo4Qr01spM8SS2BfKul3BUr2r7GkKuTOa0cNLFmmubKM14WSSWEtpJZm0An7rRzddN2oyc3A2SSI4SyTuJBDCisd9VomzXvmC1-ZW3Ms-Z0JnLjBUuKbijKQcxhDyFxwUxMmzkA0pur43J8GtOZcRgJRfpTRLAcSfYvNXTbc4QRgljaawCeL97jBpGyyZFbVfXvg6yIoQN1nnV4GD3Ux2aAkj3ELLXl_0nCGqfxbsFcQCfOyzddesvQxV5qP17QPPp91Fz9-a_-_QWHlFzzZbLYzi62lzbd8i9rsoeHDI-w2s6T3vwYHR6PvuGn8Zy3PP_ZuB1yrOe18g_SVIxhw
link.rule.ids 230,315,730,783,787,867,888,2109,11574,12068,21400,24330,27936,27937,31731,31732,33756,33757,41132,42201,43322,43817,46064,46488,50826,50935,51588,53804,53806
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELagCMEF8SxbCgSE4BTV8dpOfEJbRLXAbi-00l6Q5fjBrkSy201b0X_PTF5VVNFb5FecedjfxOMZQj5YFpTyEjQtAduEu5DHOacuNjTNx06lNnF4UXh-LKen_PtCLNofblXrVtmtifVC7dYW_5EfMIAqCWMpVZ83ZzFmjcLT1TaFxl1yD-NwYQaDdNEbXLgZsTaupmCCHRRVjs5cGaAMOdiH6nD9sLss0RnyJtK86TDZn5oOMW29KR09Jo9aNBlNGvY_IXd8-ZTcb_JLXj0jvyaRRW_p7aV3UeHxku-qKiK3xViz0QalBvkS1X7l_m8EQNoX-Z-rCMryJowzjG6X6LJXrQvoY0oXbQBwFytXPSenR19PvkzjNp9CbCVLZewyyj1CBi9hhVM0UOcV6KuRVojMjIMF2w7sodQB4TKnRDBgreWZ4gn1BnDXC7JTrkv_kkRcuSxYEWSgllufKMt4bhKPAe0k835EPnbU1ZsmbIZGcwPZoIENumPDiBwi7ftGGO26Llhvf-tWeTQTNguZ8yIkhgdcckCGAKdwahCRwSDvgXODMaaTmcYyRLCSi_QyGZH9jrG61dNKX0vViLzrq0HD8NjElH59UbcBVEQ5hza7jRz0rxrjebhQUJMOJGQwl2FNuVrWUbwlgqUx9PzUydL1tP5DqrgWtdsJquc_D5unvds_-C15MD2Zz_Ts2_GPV-Qh9m_uWO6TnfPthX8NYOs8f1Nr1D9iEyVh
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1baxQxFA61ovRFvHdrq1FEn4ZmspnMBJ-21WXVtgha6IuETC7uQmd22dkW--89Zy5bhkXxbchtwrkk3-FcQshby4NSXoKmxWCbCBfyKBfMRYal-dCp1MYOE4VPz-TkXHy5SC62yIcuF6aOdu9ckk1OA1ZpKleHCxe693r4YVHlGJaVAV6Qd8hdge-lo6dWHnfHMN5EvC2quTGldwnVtfrhapliJOQmzNyMlly7TPuAtr6Rxg_JgxZK0lHD-0dky5ePyb3mccmbJ-TniFoMlV5ee0cLjxm-s6qgbomFZukCRQaZQuugcv-bAor2RX55Q6Etb2o4w-p2ivF61byAOaZ0dAFou5i56ik5H3_6cTyJ2scUIit5KiOXMeERL3gJx5tigTmvQFmNtEmSmWGwYNiBMZQ6IFzmVBIMmGp5pkTMvAHQ9Yxsl_PS7xIqlMuCTYIMzArrY2W5yE3ssZqd5N4PyLuOunrR1MzQaGsgGzSwQXdsGJAjpP16EJa6rhvmy1-61RzNE5uFzPkkxEYEPG9AgACkCGYQjsEib4BzvTUmoxONbQhfpUjS63hA9jvG6lZJK80B_cacp0wNyOt1N6gX-kxM6edX9RiAREwIGPO8kYP1r4boDE8U9KQ9Centpd9TzqZ1CW-JSGkIM993snS7rb-QKqpF7d8E1affj5qvvf9e-RW5_-3jWJ98Pvv6guxga5NquU-2V8srfwCYa5W_rHXrD7TXJRM
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=A+conserved+mechanism+drives+partition+complex+assembly+on+bacterial+chromosomes+and+plasmids&rft.jtitle=Molecular+systems+biology&rft.au=Debaugny%2C+Roxanne+E&rft.au=Sanchez%2C+Aurore&rft.au=Rech%2C+J%C3%A9r%C3%B4me&rft.au=Labourdette%2C+Delphine&rft.date=2018-11-01&rft.pub=Nature+Publishing+Group+UK&rft.eissn=1744-4292&rft.volume=14&rft.issue=11&rft_id=info:doi/10.15252%2Fmsb.20188516&rft.externalDocID=10_15252_msb_20188516
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1744-4292&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1744-4292&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1744-4292&client=summon