Modifications at K31 on the lateral surface of histone H4 contribute to genome structure and expression in apicomplexan parasites

An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromat...

Full description

Saved in:
Bibliographic Details
Published ineLife Vol. 6
Main Authors Sindikubwabo, Fabien, Ding, Shuai, Hussain, Tahir, Ortet, Philippe, Barakat, Mohamed, Baumgarten, Sebastian, Cannella, Dominique, Palencia, Andrés, Bougdour, Alexandre, Belmudes, Lucid, Couté, Yohann, Tardieux, Isabelle, Botté, Cyrille Y, Scherf, Artur, Hakimi, Mohamed-ali
Format Journal Article
LanguageEnglish
Published England eLife Science Publications, Ltd 04.11.2017
eLife Sciences Publications Ltd
eLife Sciences Publication
eLife Sciences Publications, Ltd
Subjects
Acetylation
Animals
Apicomplexa
Biochemistry
Cellular Biology
Chromatin
Chromosomes
Deoxyribonucleic acid
DNA
DNA methylation
Enzymes
Epigenesis, Genetic
Euchromatin
Gene expression
Genes
Genetic aspects
Genetics
Genomes
Genomics
Heterochromatin
Heterochromatin - metabolism
histone core modifications
Histone H4
Histones - metabolism
Life Sciences
Malaria
methylation
Microbiology and Infectious Disease
Microbiology and Parasitology
Parasites
Parasitology
Pathogenic microorganisms
Plasmodium falciparum
Plasmodium falciparum - genetics
Plasmodium falciparum - physiology
Protein Processing, Post-Translational
Proteins
RNA polymerase
Scientific equipment industry
Structure (Literature)
Subcellular Processes
Toxoplasma - genetics
Toxoplasma - physiology
Toxoplasma gondii
Transcription
Transcription (Genetics)
Canada
United States
acetylation
Toxoplasma gondii
infectious disease
methylation
histone core modifications
microbiology
chromatin
gene expression
Online AccessGet full text

Cover

Abstract An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromatin shapers include histone modifications at the nucleosome lateral surface close to the DNA but their mode of action remains unclear. We now identify versatile modifications at Lys31 within the globular domain of histone H4 that crucially determine genome organization and expression in Apicomplexa parasites. H4K31 acetylation at the promoter correlates with, and perhaps directly regulates, gene expression in both parasites. By contrast, monomethylated H4K31 is enriched in the core body of T. gondii active genes but inversely correlates with transcription, whereas it is unexpectedly enriched at transcriptionally inactive pericentromeric heterochromatin in P. falciparum, a region devoid of the characteristic H3K9me3 histone mark and its downstream effector HP1.
AbstractList An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromatin shapers include histone modifications at the nucleosome lateral surface close to the DNA but their mode of action remains unclear. We now identify versatile modifications at Lys31 within the globular domain of histone H4 that crucially determine genome organization and expression in Apicomplexa parasites. H4K31 acetylation at the promoter correlates with, and perhaps directly regulates, gene expression in both parasites. By contrast, monomethylated H4K31 is enriched in the core body of T. gondii active genes but inversely correlates with transcription, whereas it is unexpectedly enriched at transcriptionally inactive pericentromeric heterochromatin in P. falciparum, a region devoid of the characteristic H3K9me3 histone mark and its downstream effector HP1.
An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromatin shapers include histone modifications at the nucleosome lateral surface close to the DNA but their mode of action remains unclear. We now identify versatile modifications at Lys31 within the globular domain of histone H4 that crucially determine genome organization and expression in Apicomplexa parasites. H4K31 acetylation at the promoter correlates with, and perhaps directly regulates, gene expression in both parasites. By contrast, monomethylated H4K31 is enriched in the core body of T. gondii active genes but inversely correlates with transcription, whereas it is unexpectedly enriched at transcriptionally inactive pericentromeric heterochromatin in P. falciparum, a region devoid of the characteristic H3K9me3 histone mark and its downstream effector HP1.An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromatin shapers include histone modifications at the nucleosome lateral surface close to the DNA but their mode of action remains unclear. We now identify versatile modifications at Lys31 within the globular domain of histone H4 that crucially determine genome organization and expression in Apicomplexa parasites. H4K31 acetylation at the promoter correlates with, and perhaps directly regulates, gene expression in both parasites. By contrast, monomethylated H4K31 is enriched in the core body of T. gondii active genes but inversely correlates with transcription, whereas it is unexpectedly enriched at transcriptionally inactive pericentromeric heterochromatin in P. falciparum, a region devoid of the characteristic H3K9me3 histone mark and its downstream effector HP1.
An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromatin shapers include histone modifications at the nucleosome lateral surface close to the DNA but their mode of action remains unclear. We now identify versatile modifications at Lys31 within the globular domain of histone H4 that crucially determine genome organization and expression in Apicomplexa parasites. H4K31 acetylation at the promoter correlates with, and perhaps directly regulates, gene expression in both parasites. By contrast, monomethylated H4K31 is enriched in the core body of T. gondii active genes but inversely correlates with transcription, whereas it is unexpectedly enriched at transcriptionally inactive pericentromeric heterochromatin in P. falciparum , a region devoid of the characteristic H3K9me3 histone mark and its downstream effector HP1.
An unusual genome architecture characterizes the two related human parasitic pathogens and A major fraction of the bulk parasite genome is packaged as transcriptionally permissive euchromatin with few loci embedded in silenced heterochromatin. Primary chromatin shapers include histone modifications at the nucleosome lateral surface close to the DNA but their mode of action remains unclear. We now identify versatile modifications at Lys31 within the globular domain of histone H4 that crucially determine genome organization and expression in Apicomplexa parasites. H4K31 acetylation at the promoter correlates with, and perhaps directly regulates, gene expression in both parasites. By contrast, monomethylated H4K31 is enriched in the core body of active genes but inversely correlates with transcription, whereas it is unexpectedly enriched at transcriptionally inactive pericentromeric heterochromatin in , a region devoid of the characteristic H3K9me3 histone mark and its downstream effector HP1.
Audience Academic
Author Tardieux, Isabelle
Palencia, Andrés
Hakimi, Mohamed-ali
Belmudes, Lucid
Bougdour, Alexandre
Couté, Yohann
Cannella, Dominique
Scherf, Artur
Botté, Cyrille Y
Ortet, Philippe
Ding, Shuai
Baumgarten, Sebastian
Sindikubwabo, Fabien
Hussain, Tahir
Barakat, Mohamed
Author_xml – sequence: 1
  givenname: Fabien
  surname: Sindikubwabo
  fullname: Sindikubwabo, Fabien
  organization: Institute for Advanced Biosciences (IAB), Team Host-pathogen interactions and immunity to infection, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 2
  givenname: Shuai
  surname: Ding
  fullname: Ding, Shuai
  organization: Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, CNRS, ERL 9195, INSERM, Unit U1201, Paris, France
– sequence: 3
  givenname: Tahir
  surname: Hussain
  fullname: Hussain, Tahir
  organization: Institute for Advanced Biosciences (IAB), Team Host-pathogen interactions and immunity to infection, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 4
  givenname: Philippe
  surname: Ortet
  fullname: Ortet, Philippe
  organization: Aix-Marseille Univ, CEA, CNRS, UMR 7265, BIAM-LEMIRE, St-Paul-lez-Durance, France
– sequence: 5
  givenname: Mohamed
  surname: Barakat
  fullname: Barakat, Mohamed
  organization: Aix-Marseille Univ, CEA, CNRS, UMR 7265, BIAM-LEMIRE, St-Paul-lez-Durance, France
– sequence: 6
  givenname: Sebastian
  surname: Baumgarten
  fullname: Baumgarten, Sebastian
  organization: Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, CNRS, ERL 9195, INSERM, Unit U1201, Paris, France
– sequence: 7
  givenname: Dominique
  surname: Cannella
  fullname: Cannella, Dominique
  organization: Institute for Advanced Biosciences (IAB), Team Host-pathogen interactions and immunity to infection, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 8
  givenname: Andrés
  orcidid: 0000-0002-1805-319X
  surname: Palencia
  fullname: Palencia, Andrés
  organization: Institute for Advanced Biosciences (IAB), Team Host-pathogen interactions and immunity to infection, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 9
  givenname: Alexandre
  surname: Bougdour
  fullname: Bougdour, Alexandre
  organization: Institute for Advanced Biosciences (IAB), Team Host-pathogen interactions and immunity to infection, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 10
  givenname: Lucid
  surname: Belmudes
  fullname: Belmudes, Lucid
  organization: Université Grenoble Alpes, CEA, INSERM, Grenoble, France
– sequence: 11
  givenname: Yohann
  orcidid: 0000-0003-3896-6196
  surname: Couté
  fullname: Couté, Yohann
  organization: Université Grenoble Alpes, CEA, INSERM, Grenoble, France
– sequence: 12
  givenname: Isabelle
  surname: Tardieux
  fullname: Tardieux, Isabelle
  organization: Institute for Advanced Biosciences (IAB), Team Membrane and Cell Dynamics of Host Parasite Interactions, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 13
  givenname: Cyrille Y
  surname: Botté
  fullname: Botté, Cyrille Y
  organization: Institute for Advanced Biosciences (IAB), Team ApicoLipid, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
– sequence: 14
  givenname: Artur
  surname: Scherf
  fullname: Scherf, Artur
  organization: Unité de Biologie des Interactions Hôte-Parasite, Institut Pasteur, CNRS, ERL 9195, INSERM, Unit U1201, Paris, France
– sequence: 15
  givenname: Mohamed-ali
  orcidid: 0000-0002-2547-8233
  surname: Hakimi
  fullname: Hakimi, Mohamed-ali
  organization: Institute for Advanced Biosciences (IAB), Team Host-pathogen interactions and immunity to infection, INSERM U1209, CNRS UMR5309, Université Grenoble Alpes, Grenoble, France
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29101771$$D View this record in MEDLINE/PubMed
https://hal.science/hal-02022719$$DView record in HAL
BookMark eNptks1v0zAYhyM0xMbYiTuyxAWEOmwnTuwLUjUBrShC4kPiZrnO69ZVame2M40j_znux6CtyCWW87yPX7_5PS3OnHdQFM8Jvm4Yq97CzBq4pqIU5FFxQTHDI8yrn2cH6_PiKsYVzk9TcU7Ek-KcCoJJ05CL4vdn31pjtUrWu4hUQp9KgrxDaQmoUwmC6lAcglEakDdoaWPKHaBJhbR3Kdj5kAAljxbg_BpQTGHQaQiAlGsR3PcBYsxqZB1SvdV-3XdwrxzqVVDRJojPisdGdRGu9u_L4seH999vJqPZl4_Tm_FspFlD0qgyxpRCt7jmtaB53QDUpVas5txUjDBNWlMrOmetwo1iFTecsIaVmOS6FpeXxXTnbb1ayT7YtQq_pFdWbjd8WEgVktUdSCpUVc8rJjDJHsC8JsCNoFQDqQhtsuvdztUP8zW0GvIkVHckPf7i7FIu_J3M3TJGyix4vRMsT8om45nc7GGKKW2IuCOZfbU_LPjbAWKSaxs1dJ1y4IcoiaixyE3xKqMvT9CVH4LLY81UgxnnAvN_1ELly1pnfO5Rb6RyXNOyrkh52OKe2vxuuE8LNcQop9--HrMvDufx90YPOcsA2QE6-BgDGKlt2mYuH207SbDcxFlu4yy3cc41b05qHrT_o_8AYsHz-A
CitedBy_id crossref_primary_10_1007_s13361_019_02219_1
crossref_primary_10_1016_j_fgb_2023_103800
crossref_primary_10_1016_j_mib_2024_102472
crossref_primary_10_1016_j_matbio_2018_02_015
crossref_primary_10_1128_mbio_03573_22
crossref_primary_10_1128_spectrum_03891_22
crossref_primary_10_1002_anie_202408564
crossref_primary_10_1093_nar_gkz1044
crossref_primary_10_1002_jmv_29234
crossref_primary_10_1038_s41467_021_23477_2
crossref_primary_10_1038_s41564_020_0674_4
crossref_primary_10_1016_j_gene_2019_144155
crossref_primary_10_1186_s12864_022_08338_6
crossref_primary_10_1007_s13237_021_00356_1
crossref_primary_10_1128_spectrum_00702_22
crossref_primary_10_1360_SSV_2023_0221
crossref_primary_10_15252_embr_201846331
crossref_primary_10_3389_fphar_2023_1192999
crossref_primary_10_1146_annurev_micro_090817_062741
crossref_primary_10_1186_s12915_021_00959_9
crossref_primary_10_1016_j_xcrp_2023_101638
crossref_primary_10_1002_ange_202408564
crossref_primary_10_1016_j_molbiopara_2024_111615
crossref_primary_10_1016_j_mib_2020_09_009
crossref_primary_10_1093_femsmc_xtae034
crossref_primary_10_1136_jmg_2022_109085
crossref_primary_10_1038_s41467_024_51011_7
crossref_primary_10_1038_s41467_018_04295_5
crossref_primary_10_3390_pathogens13010033
crossref_primary_10_1016_j_xpro_2024_103527
Cites_doi 10.1586/eri.12.100
10.1016/j.ijpara.2017.04.001
10.1021/pr9000898
10.1073/pnas.0800057105
10.1016/j.cell.2008.06.018
10.1016/j.molcel.2009.07.027
10.1007/978-1-62703-026-7_23
10.1128/EC.5.1.62-76.2006
10.1186/1471-2164-15-806
10.1039/c3mb25517d
10.1016/j.celrep.2013.11.038
10.1073/pnas.0902515106
10.1021/acs.jproteome.6b00366
10.1038/srep19722
10.1038/nsmb851
10.1016/j.molbiopara.2012.06.005
10.1021/pr050188r
10.1016/j.cell.2013.01.032
10.1038/nsmb.2581
10.1016/j.tcb.2014.08.007
10.1016/j.str.2015.02.011
10.1038/383269a0
10.1128/MCB.25.22.10060-10070.2005
10.1016/j.chom.2008.12.012
10.1021/pr500992r
10.1534/g3.113.005926
10.1371/journal.ppat.1000569
10.1038/35039531
10.1002/pmic.201400075
10.1111/j.1462-5822.2010.01446.x
10.1128/MCB.00441-15
10.1074/jbc.M607909200
10.1101/gad.219626.113
10.1016/j.cell.2012.02.013
10.1093/nar/gkm1057
10.1021/bi201021h
10.1128/EC.00088-12
10.1111/j.1462-5822.2012.01803.x
10.1074/mcp.M111.015875
10.1084/jem.20082826
10.1038/nsmb.1629
10.1016/j.mib.2014.05.007
10.1186/1471-2164-13-424
10.1038/ncomms11191
10.1371/journal.pone.0134586
10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X
10.1186/1741-7007-3-26
10.1146/annurev.micro.61.080706.093134
10.1016/j.tig.2015.10.007
10.1186/s12864-015-1225-x
10.1007/978-1-62703-026-7_24
10.1371/journal.pbio.0000005
10.1128/mSphere.00347-16
10.1074/jbc.M607900200
10.1016/j.chom.2013.03.002
10.1073/pnas.1006741108
10.7554/eLife.01632
10.1128/mBio.00922-13
10.1038/47412
10.1371/journal.pone.0032671
10.1128/MCB.00482-07
10.1016/j.molcel.2011.07.032
ContentType Journal Article
Copyright COPYRIGHT 2017 eLife Science Publications, Ltd.
2017, Sindikubwabo et al. This work is licensed under the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/3.0/ ) (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Attribution
2017, Sindikubwabo et al 2017 Sindikubwabo et al
Copyright_xml – notice: COPYRIGHT 2017 eLife Science Publications, Ltd.
– notice: 2017, Sindikubwabo et al. This work is licensed under the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/3.0/ ) (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: Attribution
– notice: 2017, Sindikubwabo et al 2017 Sindikubwabo et al
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
ISR
3V.
7X7
7XB
88E
88I
8FE
8FH
8FI
8FJ
8FK
ABUWG
AFKRA
AZQEC
BBNVY
BENPR
BHPHI
CCPQU
DWQXO
FYUFA
GHDGH
GNUQQ
HCIFZ
K9.
LK8
M0S
M1P
M2P
M7P
PHGZM
PHGZT
PIMPY
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
Q9U
7X8
1XC
VOOES
5PM
DOA
DOI 10.7554/eLife.29391
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
Gale In Context: Science
ProQuest Central (Corporate)
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
Science Database (Alumni Edition)
ProQuest SciTech Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Natural Science Collection
ProQuest One Community College
ProQuest Central Korea
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
ProQuest Health & Medical Collection
Medical Database
Science Database
Biological Science Database
ProQuest Central Premium
ProQuest One Academic
Publicly Available Content Database
ProQuest Health & Medical Research Collection
ProQuest One Academic Middle East (New)
ProQuest One Health & Nursing
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
ProQuest Central Basic
MEDLINE - Academic
Hyper Article en Ligne (HAL)
Hyper Article en Ligne (HAL) (Open Access)
PubMed Central (Full Participant titles)
Directory of Open Access Journals - May need to register for free articles
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
Publicly Available Content Database
ProQuest Central Student
ProQuest One Academic Middle East (New)
ProQuest Central Essentials
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
SciTech Premium Collection
ProQuest One Community College
ProQuest One Health & Nursing
ProQuest Natural Science Collection
ProQuest Central China
ProQuest Central
ProQuest One Applied & Life Sciences
ProQuest Health & Medical Research Collection
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
Natural Science Collection
ProQuest Central Korea
Health & Medical Research Collection
Biological Science Collection
ProQuest Central (New)
ProQuest Medical Library (Alumni)
ProQuest Science Journals (Alumni Edition)
ProQuest Biological Science Collection
ProQuest Central Basic
ProQuest Science Journals
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
Biological Science Database
ProQuest SciTech Collection
ProQuest Hospital Collection (Alumni)
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
ProQuest One Academic
ProQuest One Academic (New)
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList

CrossRef
MEDLINE - Academic

Publicly Available Content Database
MEDLINE
Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  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: 3
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 4
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2050-084X
ExternalDocumentID oai_doaj_org_article_29a46b45901548e0861e8f922ce14127
PMC5685513
oai_HAL_hal_02022719v1
A623641313
29101771
10_7554_eLife_29391
Genre Research Support, Non-U.S. Gov't
Journal Article
GeographicLocations Canada
United States
GeographicLocations_xml – name: Canada
– name: United States
GrantInformation_xml – fundername: ;
  grantid: ERC AdG No. 670301
– fundername: ;
  grantid: ERC Consolidator Grant No. 614880
– fundername: ;
  grantid: ANR-12-PDOC-0028
– fundername: ;
  grantid: LABEX PARAFRAP ANR-11-LABX-0024
– fundername: ;
  grantid: ANR-10-INBS-08-01
– fundername: ;
  grantid: Atip-Avenir Program Project Apicolipid
– fundername: ;
  grantid: ANR-12-BSV3-0009-01
GroupedDBID 53G
5VS
7X7
88E
88I
8FE
8FH
8FI
8FJ
AAFWJ
AAKDD
AAYXX
ABUWG
ACGFO
ACGOD
ACPRK
ADBBV
ADRAZ
AENEX
AFKRA
AFPKN
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
AZQEC
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
BPHCQ
BVXVI
CCPQU
CITATION
DIK
DWQXO
EMOBN
FYUFA
GNUQQ
GROUPED_DOAJ
GX1
HCIFZ
HMCUK
HYE
IAO
IEA
IHR
INH
INR
ISR
ITC
KQ8
LK8
M1P
M2P
M48
M7P
M~E
NQS
OK1
PGMZT
PHGZM
PHGZT
PIMPY
PQQKQ
PROAC
PSQYO
RHI
RNS
RPM
UKHRP
CGR
CUY
CVF
ECM
EIF
NPM
PJZUB
PPXIY
PQGLB
3V.
7XB
8FK
K9.
PKEHL
PQEST
PQUKI
PRINS
PUEGO
Q9U
7X8
1XC
PMFND
VOOES
5PM
ID FETCH-LOGICAL-c571t-4fff39cd068692ff37ee63ca5688f4515c1df6a2b5da07a548f81575301f39d03
IEDL.DBID M48
ISSN 2050-084X
IngestDate Wed Aug 27 01:30:14 EDT 2025
Thu Aug 21 18:04:24 EDT 2025
Tue Jun 03 06:27:35 EDT 2025
Fri Jul 11 00:33:51 EDT 2025
Mon Aug 25 14:14:56 EDT 2025
Tue Jun 17 21:08:33 EDT 2025
Fri Jun 27 04:43:49 EDT 2025
Mon Jul 21 06:04:53 EDT 2025
Tue Jul 01 04:07:44 EDT 2025
Thu Apr 24 22:59:47 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Keywords acetylation
Toxoplasma gondii
infectious disease
methylation
histone core modifications
microbiology
chromatin
gene expression
Language English
License http://creativecommons.org/licenses/by/4.0
Attribution: http://creativecommons.org/licenses/by
This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c571t-4fff39cd068692ff37ee63ca5688f4515c1df6a2b5da07a548f81575301f39d03
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
PMCID: PMC5685513
ORCID 0000-0002-1805-319X
0000-0003-3896-6196
0000-0002-2547-8233
0000-0002-1665-9833
0000-0003-2646-7699
0000-0002-5677-7463
0000-0002-2245-536X
0000-0002-3515-0055
0000-0002-2648-8978
0000-0003-2411-3328
OpenAccessLink http://journals.scholarsportal.info/openUrl.xqy?doi=10.7554/eLife.29391
PMID 29101771
PQID 1970588908
PQPubID 2045579
ParticipantIDs doaj_primary_oai_doaj_org_article_29a46b45901548e0861e8f922ce14127
pubmedcentral_primary_oai_pubmedcentral_nih_gov_5685513
hal_primary_oai_HAL_hal_02022719v1
proquest_miscellaneous_1960927384
proquest_journals_1970588908
gale_infotracmisc_A623641313
gale_incontextgauss_ISR_A623641313
pubmed_primary_29101771
crossref_citationtrail_10_7554_eLife_29391
crossref_primary_10_7554_eLife_29391
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2017-11-04
PublicationDateYYYYMMDD 2017-11-04
PublicationDate_xml – month: 11
  year: 2017
  text: 2017-11-04
  day: 04
PublicationDecade 2010
PublicationPlace England
PublicationPlace_xml – name: England
– name: Cambridge
PublicationTitle eLife
PublicationTitleAlternate Elife
PublicationYear 2017
Publisher eLife Science Publications, Ltd
eLife Sciences Publications Ltd
eLife Sciences Publication
eLife Sciences Publications, Ltd
Publisher_xml – name: eLife Science Publications, Ltd
– name: eLife Sciences Publications Ltd
– name: eLife Sciences Publication
– name: eLife Sciences Publications, Ltd
References Williams (bib58) 2008; 105
Freitas-Junior (bib15) 2000; 407
Tropberger (bib53) 2013; 20
Kim (bib27) 2013; 5
Soldi (bib49) 2014; 14
Xue (bib61) 2013; 9
Radke (bib41) 2005; 3
Trelle (bib51) 2009; 8
Vanagas (bib55) 2012; 10
Gissot (bib18) 2012; 7
Kuo (bib28) 1996; 383
Turner (bib54) 2000; 22
Mancio-Silva (bib34) 2013; 923
Cobbold (bib9) 2016; 6
Sautel (bib46) 2007; 27
Morris (bib36) 2007; 282
Brooks (bib7) 2011; 108
Hyland (bib22) 2005; 25
Scherf (bib47) 2008; 62
Hoeijmakers (bib20) 2012; 14
Hehl (bib19) 2015; 16
Karmodiya (bib26) 2012; 13
Bougdour (bib4) 2013; 13
Sierra-Miranda (bib48) 2012; 185
Wisniewski (bib59) 2008; 36
Li (bib30) 2008; 134
Li (bib31) 2014; 13
Hong (bib21) 2017; 2
Jain (bib24) 2015; 23
Saraf (bib45) 2016; 15
Pittman (bib40) 2014; 15
Salcedo-Amaya (bib43) 2009; 106
Nguyen (bib39) 2013; 3
Voss (bib57) 2014; 20
Tropberger (bib52) 2013; 152
Di Cerbo (bib12) 2014; 3
Ramakrishnan (bib42) 2017; 47
Lopez-Rubio (bib32) 2009; 5
Bhatti (bib2) 2006; 5
Strahl (bib50) 2000; 403
Xie (bib60) 2012; 11
Filippakopoulos (bib13) 2012; 149
Lopez-Rubio (bib33) 2013; 923
Sangaré (bib44) 2016; 7
Iwasaki (bib23) 2011; 50
Daujat (bib11) 2009; 16
Nardelli (bib37) 2013; 4
Cosgrove (bib10) 2004; 11
Neumann (bib38) 2009; 36
Bougdour (bib5) 2009; 206
Bozdech (bib6) 2003; 1
Jeffers (bib25) 2012; 11
Moraes (bib35) 2015; 10
Voigt (bib56) 2013; 27
Bougdour (bib3) 2010; 12
Garcia (bib17) 2007; 282
Flueck (bib14) 2009; 5
Lawrence (bib29) 2016; 32
Chatterjee (bib8) 2015; 35
Azzalin (bib1) 2015; 25
Yang (bib62) 2011; 44
Garcia (bib16) 2005; 4
References_xml – volume: 10
  start-page: 1189
  year: 2012
  ident: bib55
  article-title: Toxoplasma histone acetylation remodelers as novel drug targets
  publication-title: Expert Review of Anti-Infective Therapy
  doi: 10.1586/eri.12.100
– volume: 47
  start-page: 597
  year: 2017
  ident: bib42
  article-title: The merozoite-specific protein, TgGRA11B, identified as a component of the Toxoplasma gondii parasitophorous vacuole in a tachyzoite expression model
  publication-title: International Journal for Parasitology
  doi: 10.1016/j.ijpara.2017.04.001
– volume: 8
  start-page: 3439
  year: 2009
  ident: bib51
  article-title: Global histone analysis by mass spectrometry reveals a high content of acetylated lysine residues in the malaria parasite Plasmodium falciparum
  publication-title: Journal of Proteome Research
  doi: 10.1021/pr9000898
– volume: 105
  start-page: 9000
  year: 2008
  ident: bib58
  article-title: Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation
  publication-title: PNAS
  doi: 10.1073/pnas.0800057105
– volume: 134
  start-page: 244
  year: 2008
  ident: bib30
  article-title: Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
  publication-title: Cell
  doi: 10.1016/j.cell.2008.06.018
– volume: 36
  start-page: 153
  year: 2009
  ident: bib38
  article-title: A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation
  publication-title: Molecular Cell
  doi: 10.1016/j.molcel.2009.07.027
– volume: 923
  start-page: 321
  year: 2013
  ident: bib33
  article-title: Genome-wide chromatin immunoprecipitation-sequencing in Plasmodium
  publication-title: Methods in Molecular Biology
  doi: 10.1007/978-1-62703-026-7_23
– volume: 5
  start-page: 62
  year: 2006
  ident: bib2
  article-title: Pair of unusual GCN5 histone acetyltransferases and ADA2 homologues in the protozoan parasite Toxoplasma gondii
  publication-title: Eukaryotic Cell
  doi: 10.1128/EC.5.1.62-76.2006
– volume: 15
  start-page: 806
  year: 2014
  ident: bib40
  article-title: Dual transcriptional profiling of mice and Toxoplasma gondii during acute and chronic infection
  publication-title: BMC Genomics
  doi: 10.1186/1471-2164-15-806
– volume: 9
  start-page: 645
  year: 2013
  ident: bib61
  article-title: Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii
  publication-title: Molecular BioSystems
  doi: 10.1039/c3mb25517d
– volume: 5
  start-page: 1690
  year: 2013
  ident: bib27
  article-title: Linker Histone H1.2 cooperates with Cul4A and PAF1 to drive H4K31 ubiquitylation-mediated transactivation
  publication-title: Cell Reports
  doi: 10.1016/j.celrep.2013.11.038
– volume: 106
  start-page: 9655
  year: 2009
  ident: bib43
  article-title: Dynamic histone H3 epigenome marking during the intraerythrocytic cycle of Plasmodium falciparum
  publication-title: PNAS
  doi: 10.1073/pnas.0902515106
– volume: 15
  start-page: 2787
  year: 2016
  ident: bib45
  article-title: Dynamic and combinatorial landscape of histone modifications during the intraerythrocytic developmental cycle of the malaria parasite
  publication-title: Journal of Proteome Research
  doi: 10.1021/acs.jproteome.6b00366
– volume: 6
  start-page: 19722
  year: 2016
  ident: bib9
  article-title: Proteome-wide analysis reveals widespread lysine acetylation of major protein complexes in the malaria parasite
  publication-title: Scientific Reports
  doi: 10.1038/srep19722
– volume: 11
  start-page: 1037
  year: 2004
  ident: bib10
  article-title: Regulated nucleosome mobility and the histone code
  publication-title: Nature Structural & Molecular Biology
  doi: 10.1038/nsmb851
– volume: 185
  start-page: 36
  year: 2012
  ident: bib48
  article-title: Two long non-coding RNAs generated from subtelomeric regions accumulate in a novel perinuclear compartment in Plasmodium falciparum
  publication-title: Molecular and Biochemical Parasitology
  doi: 10.1016/j.molbiopara.2012.06.005
– volume: 4
  start-page: 2032
  year: 2005
  ident: bib16
  article-title: Resetting the epigenetic histone code in the MRL-lpr/lpr mouse model of lupus by histone deacetylase inhibition
  publication-title: Journal of Proteome Research
  doi: 10.1021/pr050188r
– volume: 152
  start-page: 859
  year: 2013
  ident: bib52
  article-title: Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer
  publication-title: Cell
  doi: 10.1016/j.cell.2013.01.032
– volume: 20
  start-page: 657
  year: 2013
  ident: bib53
  article-title: Scratching the (lateral) surface of chromatin regulation by histone modifications
  publication-title: Nature Structural & Molecular Biology
  doi: 10.1038/nsmb.2581
– volume: 25
  start-page: 29
  year: 2015
  ident: bib1
  article-title: Telomere functions grounding on TERRA firma
  publication-title: Trends in Cell Biology
  doi: 10.1016/j.tcb.2014.08.007
– volume: 23
  start-page: 819
  year: 2015
  ident: bib24
  article-title: Structure of prolyl-trna synthetase-halofuginone complex provides basis for development of drugs against malaria and toxoplasmosis
  publication-title: Structure
  doi: 10.1016/j.str.2015.02.011
– volume: 383
  start-page: 269
  year: 1996
  ident: bib28
  article-title: Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
  publication-title: Nature
  doi: 10.1038/383269a0
– volume: 25
  start-page: 10060
  year: 2005
  ident: bib22
  article-title: Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae
  publication-title: Molecular and Cellular Biology
  doi: 10.1128/MCB.25.22.10060-10070.2005
– volume: 5
  start-page: 179
  year: 2009
  ident: bib32
  article-title: Genome-wide analysis of heterochromatin associates clonally variant gene regulation with perinuclear repressive centers in malaria parasites
  publication-title: Cell Host & Microbe
  doi: 10.1016/j.chom.2008.12.012
– volume: 13
  start-page: 6087
  year: 2014
  ident: bib31
  article-title: Systematic identification of the lysine succinylation in the protozoan parasite Toxoplasma gondii
  publication-title: Journal of Proteome Research
  doi: 10.1021/pr500992r
– volume: 3
  start-page: 929
  year: 2013
  ident: bib39
  article-title: A nucleosomal region important for ensuring proper interactions between the transcription elongation factor spt16 and transcribed genes in saccharomyces cerevisiae
  publication-title: G3: Genes,Genomes,Genetics
  doi: 10.1534/g3.113.005926
– volume: 5
  start-page: e1000569
  year: 2009
  ident: bib14
  article-title: Plasmodium falciparum heterochromatin protein 1 marks genomic loci linked to phenotypic variation of exported virulence factors
  publication-title: PLoS Pathogens
  doi: 10.1371/journal.ppat.1000569
– volume: 407
  start-page: 1018
  year: 2000
  ident: bib15
  article-title: Frequent ectopic recombination of virulence factor genes in telomeric chromosome clusters of P. falciparum
  publication-title: Nature
  doi: 10.1038/35039531
– volume: 14
  start-page: 2212
  year: 2014
  ident: bib49
  article-title: Improved bottom-up strategy to efficiently separate hypermodified histone peptides through ultra-HPLC separation on a bench top Orbitrap instrument
  publication-title: Proteomics
  doi: 10.1002/pmic.201400075
– volume: 12
  start-page: 413
  year: 2010
  ident: bib3
  article-title: Chromatin modifications: implications in the regulation of gene expression in Toxoplasma gondii
  publication-title: Cellular Microbiology
  doi: 10.1111/j.1462-5822.2010.01446.x
– volume: 35
  start-page: 4083
  year: 2015
  ident: bib8
  article-title: Histone acetylation near the nucleosome dyad axis enhances nucleosome disassembly by RSC and SWI/SNF
  publication-title: Molecular and Cellular Biology
  doi: 10.1128/MCB.00441-15
– volume: 282
  start-page: 7632
  year: 2007
  ident: bib36
  article-title: Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M607909200
– volume: 27
  start-page: 1318
  year: 2013
  ident: bib56
  article-title: A double take on bivalent promoters
  publication-title: Genes & Development
  doi: 10.1101/gad.219626.113
– volume: 149
  start-page: 214
  year: 2012
  ident: bib13
  article-title: Histone recognition and large-scale structural analysis of the human bromodomain family
  publication-title: Cell
  doi: 10.1016/j.cell.2012.02.013
– volume: 36
  start-page: 570
  year: 2008
  ident: bib59
  article-title: Nepsilon-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
  publication-title: Nucleic Acids Research
  doi: 10.1093/nar/gkm1057
– volume: 50
  start-page: 7822
  year: 2011
  ident: bib23
  article-title: Comprehensive structural analysis of mutant nucleosomes containing lysine to glutamine (KQ) substitutions in the H3 and H4 histone-fold domains
  publication-title: Biochemistry
  doi: 10.1021/bi201021h
– volume: 11
  start-page: 735
  year: 2012
  ident: bib25
  article-title: Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii
  publication-title: Eukaryotic Cell
  doi: 10.1128/EC.00088-12
– volume: 14
  start-page: 1391
  year: 2012
  ident: bib20
  article-title: Plasmodium falciparum centromeres display a unique epigenetic makeup and cluster prior to and during schizogony
  publication-title: Cellular Microbiology
  doi: 10.1111/j.1462-5822.2012.01803.x
– volume: 11
  start-page: 100
  year: 2012
  ident: bib60
  article-title: Lysine succinylation and lysine malonylation in histones
  publication-title: Molecular & Cellular Proteomics
  doi: 10.1074/mcp.M111.015875
– volume: 206
  start-page: 953
  year: 2009
  ident: bib5
  article-title: Drug inhibition of HDAC3 and epigenetic control of differentiation in Apicomplexa parasites
  publication-title: The Journal of Experimental Medicine
  doi: 10.1084/jem.20082826
– volume: 16
  start-page: 777
  year: 2009
  ident: bib11
  article-title: H3K64 trimethylation marks heterochromatin and is dynamically remodeled during developmental reprogramming
  publication-title: Nature Structural & Molecular Biology
  doi: 10.1038/nsmb.1629
– volume: 20
  start-page: 88
  year: 2014
  ident: bib57
  article-title: Epigenetic memory takes center stage in the survival strategy of malaria parasites
  publication-title: Current Opinion in Microbiology
  doi: 10.1016/j.mib.2014.05.007
– volume: 13
  start-page: 424
  year: 2012
  ident: bib26
  article-title: H3K9 and H3K14 acetylation co-occur at many gene regulatory elements, while H3K14ac marks a subset of inactive inducible promoters in mouse embryonic stem cells
  publication-title: BMC Genomics
  doi: 10.1186/1471-2164-13-424
– volume: 7
  start-page: 11191
  year: 2016
  ident: bib44
  article-title: Unconventional endosome-like compartment and retromer complex in Toxoplasma gondii govern parasite integrity and host infection
  publication-title: Nature Communications
  doi: 10.1038/ncomms11191
– volume: 10
  start-page: e0134586
  year: 2015
  ident: bib35
  article-title: Analysis of histones H3 and H4 reveals novel and conserved post-translational modifications in sugarcane
  publication-title: Plos One
  doi: 10.1371/journal.pone.0134586
– volume: 22
  start-page: 836
  year: 2000
  ident: bib54
  article-title: Histone acetylation and an epigenetic code
  publication-title: BioEssays
  doi: 10.1002/1521-1878(200009)22:9<836::AID-BIES9>3.0.CO;2-X
– volume: 3
  start-page: 26
  year: 2005
  ident: bib41
  article-title: The transcriptome of Toxoplasma gondii
  publication-title: BMC Biology
  doi: 10.1186/1741-7007-3-26
– volume: 62
  start-page: 445
  year: 2008
  ident: bib47
  article-title: Antigenic variation in Plasmodium falciparum
  publication-title: Annual Review of Microbiology
  doi: 10.1146/annurev.micro.61.080706.093134
– volume: 32
  start-page: 42
  year: 2016
  ident: bib29
  article-title: Lateral thinking: how histone modifications regulate gene expression
  publication-title: Trends in Genetics
  doi: 10.1016/j.tig.2015.10.007
– volume: 16
  start-page: 66
  year: 2015
  ident: bib19
  article-title: Asexual expansion of Toxoplasma gondii merozoites is distinct from tachyzoites and entails expression of non-overlapping gene families to attach, invade, and replicate within feline enterocytes
  publication-title: BMC Genomics
  doi: 10.1186/s12864-015-1225-x
– volume: 923
  start-page: 335
  year: 2013
  ident: bib34
  article-title: In situ fluorescence visualization of transcription sites and genomic Loci in blood stages of Plasmodium falciparum
  publication-title: Methods in Molecular Biology
  doi: 10.1007/978-1-62703-026-7_24
– volume: 1
  start-page: e5
  year: 2003
  ident: bib6
  article-title: The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
  publication-title: PLoS Biology
  doi: 10.1371/journal.pbio.0000005
– volume: 2
  start-page: e00347-16
  year: 2017
  ident: bib21
  article-title: Opposing transcriptional mechanisms regulate toxoplasma development
  publication-title: mSphere
  doi: 10.1128/mSphere.00347-16
– volume: 282
  start-page: 7641
  year: 2007
  ident: bib17
  article-title: Organismal differences in post-translational modifications in histones H3 and H4
  publication-title: Journal of Biological Chemistry
  doi: 10.1074/jbc.M607900200
– volume: 13
  start-page: 489
  year: 2013
  ident: bib4
  article-title: Host cell subversion by Toxoplasma GRA16, an exported dense granule protein that targets the host cell nucleus and alters gene expression
  publication-title: Cell Host & Microbe
  doi: 10.1016/j.chom.2013.03.002
– volume: 108
  start-page: 3767
  year: 2011
  ident: bib7
  article-title: Toxoplasma gondii sequesters centromeres to a specific nuclear region throughout the cell cycle
  publication-title: PNAS
  doi: 10.1073/pnas.1006741108
– volume: 3
  start-page: e01632
  year: 2014
  ident: bib12
  article-title: Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription
  publication-title: eLife
  doi: 10.7554/eLife.01632
– volume: 4
  start-page: e00922-13
  year: 2013
  ident: bib37
  article-title: The histone code of Toxoplasma gondii comprises conserved and unique posttranslational modifications
  publication-title: mBio
  doi: 10.1128/mBio.00922-13
– volume: 403
  start-page: 41
  year: 2000
  ident: bib50
  article-title: The language of covalent histone modifications
  publication-title: Nature
  doi: 10.1038/47412
– volume: 7
  start-page: e32671
  year: 2012
  ident: bib18
  article-title: Toxoplasma gondii chromodomain protein 1 binds to heterochromatin and colocalises with centromeres and telomeres at the nuclear periphery
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0032671
– volume: 27
  start-page: 5711
  year: 2007
  ident: bib46
  article-title: SET8-mediated methylations of histone H4 lysine 20 mark silent heterochromatic domains in apicomplexan genomes
  publication-title: Molecular and Cellular Biology
  doi: 10.1128/MCB.00482-07
– volume: 44
  start-page: 39
  year: 2011
  ident: bib62
  article-title: HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 and facilitates chromatin assembly
  publication-title: Molecular Cell
  doi: 10.1016/j.molcel.2011.07.032
SSID ssj0000748819
Score 2.328386
Snippet An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the...
An unusual genome architecture characterizes the two related human parasitic pathogens and A major fraction of the bulk parasite genome is packaged as...
An unusual genome architecture characterizes the two related human parasitic pathogens Plasmodium falciparum and Toxoplasma gondii. A major fraction of the...
SourceID doaj
pubmedcentral
hal
proquest
gale
pubmed
crossref
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Enrichment Source
SubjectTerms Acetylation
Animals
Apicomplexa
Biochemistry
Cellular Biology
Chromatin
Chromosomes
Deoxyribonucleic acid
DNA
DNA methylation
Enzymes
Epigenesis, Genetic
Euchromatin
Gene expression
Genes
Genetic aspects
Genetics
Genomes
Genomics
Heterochromatin
Heterochromatin - metabolism
histone core modifications
Histone H4
Histones - metabolism
Life Sciences
Malaria
methylation
Microbiology and Infectious Disease
Microbiology and Parasitology
Parasites
Parasitology
Pathogenic microorganisms
Plasmodium falciparum
Plasmodium falciparum - genetics
Plasmodium falciparum - physiology
Protein Processing, Post-Translational
Proteins
RNA polymerase
Scientific equipment industry
Structure (Literature)
Subcellular Processes
Toxoplasma - genetics
Toxoplasma - physiology
Toxoplasma gondii
Transcription
Transcription (Genetics)
SummonAdditionalLinks – databaseName: Directory of Open Access Journals - May need to register for free articles
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELagEhIXxJvAgkzVE1Jo7DhxfFwQ1QItB6BSb5bjB11pcapmF8GRf86Mk642gMSFSxTFk-zIM_Z8yc58Q8iBEy0sISvzSsBBmMrlJsgqL7lzAQIyaxJPwcmHenEq3p1VZzutvjAnbKAHHibukCsj6lZgiSSAaw8InPkmKM6tZ4LxVEcOMW_nZSrtwRIck6mhIE9CyDz0x8vgX0JwU2wSghJT_3Y_vn6O6ZB_Ys3fUyZ3YtDRbXJrBI90Pih9h1zz8S65MbST_HGP_DzpHGb-DB_hqFnT9yWjXaQA8ujKYK3xivaby2Csp12giWs4eroQNGWsY-srT9cdReLWr54O3LKbS09NdNR_H3NmI11Gai6WKRsdy2Mo8ofjv9D9fXJ69Obz60U-tljIbSXZOhchhFJZh4UiisO59L4uranqpgkCsI5lLtSGt5UzhTRggdAwQHiwLcB9rigfkL0Imj4i1JQloL3KyyAa4QIAIdu6UMDt0gtRhIy8uJp1bUf-cWyDsdLwHoIm0slEOpkoIwdb4YuBduPvYq_QfFsR5MpOF8CD9OhB-l8elJF9NL5GNoyI6TZfzKbv9dtPH_W8Rn59VrIyI7NRKHSgtYVFaCfD--A5Ez0W82ON1wCPcy6Z-gbazq4cS487Ra-ZkkXVNKpoMvJ8O4yPx-y36LsNytSFwhoqkZGHgx9uf4or3FQlPFxOPHSiy3QkLs8TjzgYGdv7PP4fk_iE3OQIePCDu5iRPXBQ_xTg2rp9llbmL5T5O9A
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: Health & Medical Collection
  dbid: 7X7
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3db9MwELfYEBIviG8yCjLTnpDC4sSJkydUEFOBjQdgUt8sxx9bpZKUpp3gkf-cO8cNBBAvVRVf0lPufHe-3v2OkCPDa9hCWsQ5hw-uchMrJ_I4S41x4JBZ6XEKzj4Us3P-bp7PQ8KtC2WVO5voDbVpNebIj1klkrwsq6R8ufoa49Qo_Hc1jNDYI9cRugy1WszFkGMB91iCx-vb8gQ4zmN7unD2Bbi4io0ckcfrH6zy3iUWRf4dcf5ZOPmbJzq5TW6FEJJOe5nfIddsc5fc6IdKfr9Hfpy1But_-lQcVRv6PmO0bSiEenSpsON4Sbvt2iltaeuoRxxuLJ1x6uvWcQCWpZuWInzrF0t7hNnt2lLVGGq_hcrZhi4aqlYLX5OOTTIUUcTxbXX3yfnJm8-vZ3EYtBDrXLBNzJ1zWaUNtotUKXwX1haZVnlRlo5DxKOZcYVK69yoRCg45LiSQZwHxgHuM0n2gOw3wOkjQlWWQcyXW-F4yY2DcEjXxiVwu7CcJy4iz3dvXeqAQo7DMJYSTiMoIulFJL2IInI0EK968I1_k71C8Q0kiJjtL7TrCxk2IFAqXtQcW22BfwsnOWZLV6WptoyzVETkEIUvEROjwaKbC7XtOvn200c5LRBln2Usi8gkELkWuNawFfVo-RA0Z8THbHoq8RpE5WkqWHUF3E52iiWDvejkL-2OyLNhGR-PNXCNbbdIUyQVdlLxiDzs9XD4qbRC0yrg4WKkoSNexivN4tKjiYOQccjPwf_ZekxuphjQYEKdT8g-qJ59AuHYpn7q99xPFTY1LA
  priority: 102
  providerName: ProQuest
Title Modifications at K31 on the lateral surface of histone H4 contribute to genome structure and expression in apicomplexan parasites
URI https://www.ncbi.nlm.nih.gov/pubmed/29101771
https://www.proquest.com/docview/1970588908
https://www.proquest.com/docview/1960927384
https://hal.science/hal-02022719
https://pubmed.ncbi.nlm.nih.gov/PMC5685513
https://doaj.org/article/29a46b45901548e0861e8f922ce14127
Volume 6
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3db9MwELf2ISReEN8LlMpMe0JKiRMnTp5QhzYVWCc0qNQ3y_XHVqkko2nR9sh_zp2TVmTskZeqii_pyXf2_Zze_Y6QI8NnsIS0CFMOH1ylJlROpGESG-MgILPc8xSMz7PRhH-eptMdsmnG2U5gfe_RDvtJTZaLwc3P2w-w4AG_DgREw_f2bO7sAOIWVrHvQ0gS2Mpg3OJ8vyUL8FNWNPV5d-_pRCRP3L_dnnevMDvyX-h5N4Pyr5B0-pg8arEkHTbGf0J2bPmUPGi6S94-I7_HlcFEoOadHFUr-iVhtCopYD66UFh6vKD1eumUtrRy1FMPl5aOOPUJ7NgJy9JVRZHH9YelDdXsemmpKg21N20KbUnnJVXXc5-cjtUyFOnE8U_p-jmZnJ58_zgK244LoU4FW4XcOZcU2mDdSBHDd2FtlmiVZnnuOEAfzYzLVDxLjYqEgtOOyxkAPtgl4D4TJS_IXgmaHhCqkgTAX2qF4zk3DnCRnhkXwe3Cch65gLzbzLrULR05dsVYSDiWoImkN5H0JgrI0Vb4umHhuF_sGM23FUHqbH-hWl7KdiWCpOLZjGPNLehv4UjHbO6KONaWcRaLgByi8SWSY5SYfXOp1nUtP327kMMM6fZZwpKA9FohV4HWGtak7gwfgud09BgNzyReA3gex4IVv0Db3sax5MbvJStElOZ5EeUBebsdxsdjMlxpqzXKZFGBJVU8IC8bP9z-VFzgHivg4aLjoR1duiPl_MrTioORsdvPq_8xia_Jwxjxjy_a7JE9cFD7BtDbatYnu2Iq-mT_-OT860XfvwPp-9X6B6HARyE
linkProvider Scholars Portal
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEF61RQguiDeGAEtVLkimXnvttQ8IhUeVkqQHaKXcls0-2kjBDnEC9Mgf4jcyYzsGA-LWi2V5x-tRZmZndjPzDSF7hk_BhLTwYw4XrmLjKydiPwqNceCQWVrhFIyPksEJfzeJJ1vkx6YWBtMqN2titVCbQuMZ-T7LRBCnaRakLxeffewahf-ublpo1GoxtOdfYctWvjh8A_J9GoYHb49fD_ymq4CvY8FWPnfORZk2WBuRhXAvrE0ireIkTR0H966ZcYkKp7FRgVAQ0buUQVADlgDvmSCCebfJJXC8AW72xES0ZzrgjlPwsHUZoABHvW9HM2efg0vNWMfxVf0BWi-wfYZJmH9HuH8mav7m-Q6uk2tNyEr7tY7dIFs2v0ku100sz2-R7-PCYL5RffRH1YoOI0aLnEJoSecKK5zntFwvndKWFo5WCMe5pQNOqzx5bLhl6aqgCBf7ydIa0Xa9tFTlhtpvTaZuTmc5VYtZlQOPRTkUUctROuVtcnIhIrhDdnLg9B6hKoogxoytcDzlxkH4pafGBfC6sJwHziPPNr-61A3qOTbfmEvY_aCIZCUiWYnII3st8aIG-_g32SsUX0uCCN3Vg2J5KhuDB0rFkynH0l7g38LOkdnUZWGoLeMsFB7ZReFLxODIMcnnVK3LUh5-eC_7CaL6s4hFHuk1RK4ArjWYvu4M74LmdPgY9EcSn8EuIAwFy74At72NYslmfSrlL2vyyJN2GKfHnLvcFmukSYIMK7e4R-7Weth-KsxwKRcwuehoaIeX7kg-O6vQy0HI2FTo_v_ZekyuDI7HIzk6PBo-IFdDDKbwMJ_3yA6ooX0IoeBq-qiyP0o-XrTB_wSuXnGZ
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9NAEF61qUBcEG8MAZaqXJBMvPbaax8QSmmjhKRRVajUm9nso40U7BAnQI_8LX4dM7ZjCCBuvViWd7weZWZ2Zjcz3xCyp_kETEgJN-Rw4TLUrrQidANfawsOmcUlTsHROOqf8ndn4dkW-bGuhcG0yvWaWC7UOld4Rt5hifDCOE68uGPrtIjjg96b-WcXO0jhP63rdhqVigzN5VfYvhWvBwcg6xe-3zv88Lbv1h0GXBUKtnS5tTZIlMY6icSHe2FMFCgZRnFsObh6xbSNpD8JtfSEhOjexgwCHLAKeE97Acy7TXYE7opaZGf_cHx80pzwgHOOwd9WRYEC3HbHjKbWvAIHm7ANN1h2C2h8wvYFpmT-He_-mbb5mx_s3SI36wCWdiuNu022THaHXKtaWl7eJd-Pco3ZR9VBIJVLOgwYzTMKgSadSax3ntFitbBSGZpbWuIdZ4b2OS2z5rH9lqHLnCJ47CdDK3zb1cJQmWlqvtV5uxmdZlTOp2VGPJboUMQwR_kU98jplQjhPmllwOlDQmUQQMQZGmF5zLWFYExNtPXgdWE496xDXq5_9VTVGOjYimOWwl4IRZSWIkpLETlkryGeV9Af_ybbR_E1JIjXXT7IF-dpbf5AKXk04VjoC_wb2EcyE9vE95VhnPnCIbso_BQROTLU7XO5Kop08P4k7UaI8c8CFjikXRPZHLhWsBCojeFd0JwNPvrdUYrPYE_g-4IlX4Db9lqx0nq1KtJftuWQ580wTo8ZeJnJV0gTeQnWcXGHPKj0sPmUn-DCLmBysaGhG7xsjmTTixLLHISMLYYe_Z-tZ-Q6GHs6GoyHj8kNHyMrPNnnbdICLTRPIC5cTp7WBkjJx6u2-Z81fnc0
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=Modifications+at+K31+on+the+lateral+surface+of+histone+H4+contribute+to+genome+structure+and+expression+in+apicomplexan+parasites&rft.jtitle=eLife&rft.au=Fabien+Sindikubwabo&rft.au=Shuai+Ding&rft.au=Tahir+Hussain&rft.au=Philippe+Ortet&rft.date=2017-11-04&rft.pub=eLife+Sciences+Publications+Ltd&rft.eissn=2050-084X&rft.volume=6&rft_id=info:doi/10.7554%2FeLife.29391&rft.externalDBID=DOA&rft.externalDocID=oai_doaj_org_article_29a46b45901548e0861e8f922ce14127
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2050-084X&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2050-084X&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2050-084X&client=summon