Molecular and biochemical characterization of the tetralin degradation pathway in Rhodococcus sp. strain TFB
Summary The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin‐ and glucose‐grown cells was compared using the 2D‐DIG...
Saved in:
Published in | Microbial biotechnology Vol. 2; no. 2; pp. 262 - 273 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Blackwell Publishing Ltd
01.03.2009
John Wiley & Sons, Inc |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Summary
The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin‐ and glucose‐grown cells was compared using the 2D‐DIGE technique. Identification of proteins specifically expressed in tetralin‐grown cells was used to characterize a complete set of genes involved in tetralin degradation by reverse genetics. We propose a tetralin degradation pathway analogous to that described for Sphingomonas macrogolitabida strain TFA. TFB thn genes are organized into three operons; two contain all of the structural genes and are transcribed in the same direction, while the third operon, thnST, is transcribed in the opposite direction and encodes a two‐component regulatory system, whose transcription is higher in tetralin‐grown cells. In addition to tetralin induction, TFB thn structural genes are subject to glucose repression. Primer extension assays and translational thnA1::gfp and thnS::gfp fusions were used to characterize putative promoter regions. A mutational analysis of the thnA1 promoter region allowed us to define nucleotides within the cis regulatory elements that are important for the control of thn gene expression. |
---|---|
AbstractList | The tetralin biodegradation pathway in
Rhodococcus
sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin‐ and glucose‐grown cells was compared using the 2D‐DIGE technique. Identification of proteins specifically expressed in tetralin‐grown cells was used to characterize a complete set of genes involved in tetralin degradation by reverse genetics. We propose a tetralin degradation pathway analogous to that described for
Sphingomonas macrogolitabida
strain TFA. TFB
thn
genes are organized into three operons; two contain all of the structural genes and are transcribed in the same direction, while the third operon,
thnST,
is transcribed in the opposite direction and encodes a two‐component regulatory system, whose transcription is higher in tetralin‐grown cells. In addition to tetralin induction, TFB
thn
structural genes are subject to glucose repression. Primer extension assays and translational
thnA1::gfp
and
thnS::gfp
fusions were used to characterize putative promoter regions. A mutational analysis of the
thnA1
promoter region allowed us to define nucleotides within the
cis
regulatory elements that are important for the control of
thn
gene expression. The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram-positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin- and glucose-grown cells was compared using the 2D-DIGE technique. Identification of proteins specifically expressed in tetralin-grown cells was used to characterize a complete set of genes involved in tetralin degradation by reverse genetics. We propose a tetralin degradation pathway analogous to that described for Sphingomonas macrogolitabida strain TFA. TFB thn genes are organized into three operons; two contain all of the structural genes and are transcribed in the same direction, while the third operon, thnST, is transcribed in the opposite direction and encodes a two-component regulatory system, whose transcription is higher in tetralin-grown cells. In addition to tetralin induction, TFB thn structural genes are subject to glucose repression. Primer extension assays and translational thnA1::gfp and thnS::gfp fusions were used to characterize putative promoter regions. A mutational analysis of the thnA1 promoter region allowed us to define nucleotides within the cis regulatory elements that are important for the control of thn gene expression. Summary The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin‐ and glucose‐grown cells was compared using the 2D‐DIGE technique. Identification of proteins specifically expressed in tetralin‐grown cells was used to characterize a complete set of genes involved in tetralin degradation by reverse genetics. We propose a tetralin degradation pathway analogous to that described for Sphingomonas macrogolitabida strain TFA. TFB thn genes are organized into three operons; two contain all of the structural genes and are transcribed in the same direction, while the third operon, thnST, is transcribed in the opposite direction and encodes a two‐component regulatory system, whose transcription is higher in tetralin‐grown cells. In addition to tetralin induction, TFB thn structural genes are subject to glucose repression. Primer extension assays and translational thnA1::gfp and thnS::gfp fusions were used to characterize putative promoter regions. A mutational analysis of the thnA1 promoter region allowed us to define nucleotides within the cis regulatory elements that are important for the control of thn gene expression. Summary The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a proteomic approach. Relative protein expression in cell free extracts from tetralin‐ and glucose‐grown cells was compared using the 2D‐DIGE technique. Identification of proteins specifically expressed in tetralin‐grown cells was used to characterize a complete set of genes involved in tetralin degradation by reverse genetics. We propose a tetralin degradation pathway analogous to that described for Sphingomonas macrogolitabida strain TFA. TFB thn genes are organized into three operons; two contain all of the structural genes and are transcribed in the same direction, while the third operon, thnST, is transcribed in the opposite direction and encodes a two‐component regulatory system, whose transcription is higher in tetralin‐grown cells. In addition to tetralin induction, TFB thn structural genes are subject to glucose repression. Primer extension assays and translational thnA1::gfp and thnS::gfp fusions were used to characterize putative promoter regions. A mutational analysis of the thnA1 promoter region allowed us to define nucleotides within the cis regulatory elements that are important for the control of thn gene expression. |
Author | Schlömann, Michael Santero, Eduardo Camafeita, Emilio Floriano, Belén Tomás-Gallardo, Laura Calvo, Enrique |
AuthorAffiliation | 1 Centro Andaluz de Biología del Desarrollo‐CSIC, Universidad Pablo de Olavide Carretera de Utrera, Km 1. 41013‐Seville, Spain 2 Centro Nacional de Investigaciones Cardiovasculares (CNIC), Unidad de Proteómica, Madrid, Spain 3 Interdisziplinäres Ökologisches Zentrum, Technische Universität Bergakademie Freiberg, Freiberg, Germany |
AuthorAffiliation_xml | – name: 1 Centro Andaluz de Biología del Desarrollo‐CSIC, Universidad Pablo de Olavide Carretera de Utrera, Km 1. 41013‐Seville, Spain – name: 3 Interdisziplinäres Ökologisches Zentrum, Technische Universität Bergakademie Freiberg, Freiberg, Germany – name: 2 Centro Nacional de Investigaciones Cardiovasculares (CNIC), Unidad de Proteómica, Madrid, Spain |
Author_xml | – sequence: 1 givenname: Laura surname: Tomás-Gallardo fullname: Tomás-Gallardo, Laura organization: Centro Andaluz de Biología del Desarrollo-CSIC, Universidad Pablo de Olavide Carretera de Utrera, Km 1. 41013-Seville, Spain – sequence: 2 givenname: Eduardo surname: Santero fullname: Santero, Eduardo organization: Centro Andaluz de Biología del Desarrollo-CSIC, Universidad Pablo de Olavide Carretera de Utrera, Km 1. 41013-Seville, Spain – sequence: 3 givenname: Emilio surname: Camafeita fullname: Camafeita, Emilio organization: Centro Nacional de Investigaciones Cardiovasculares (CNIC), Unidad de Proteómica, Madrid, Spain – sequence: 4 givenname: Enrique surname: Calvo fullname: Calvo, Enrique organization: Centro Nacional de Investigaciones Cardiovasculares (CNIC), Unidad de Proteómica, Madrid, Spain – sequence: 5 givenname: Michael surname: Schlömann fullname: Schlömann, Michael organization: Interdisziplinäres Ökologisches Zentrum, Technische Universität Bergakademie Freiberg, Freiberg, Germany – sequence: 6 givenname: Belén surname: Floriano fullname: Floriano, Belén email: bflopar@upo.es organization: Centro Andaluz de Biología del Desarrollo-CSIC, Universidad Pablo de Olavide Carretera de Utrera, Km 1. 41013-Seville, Spain |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21261920$$D View this record in MEDLINE/PubMed |
BookMark | eNqNUV1v0zAUtdAQ-4C_gCzxnMx2EjuWEBKd2IbohjQV9njlOs7iksbFTrZ2vx6HjGq8zS--uufjHukco4POdQYhTElK4ztdpVQUNBGSFikjRKaEkJKn21foaA8cPJsP0XEIK0I4IQV7gw4ZZZxKRo5Qe-Vao4dWeay6Ci-t041ZW61arBvlle6Nt4-qt67DrsZ9Y3Bveq9a2-HK3HlVTdhG9c2D2uG4vmlc5bTTegg4bFIcIj2uF-ezt-h1rdpg3j39J-jH-ZfF2WUy_37x9ezzPNGc5DyhvJa8IFRISaXMVdxxmeeSMSaKrMqFYlJVVWlEWS6ZyEWENeV5nbOKZoJkJ-jT5LsZlmtTadONiWHj7Vr5HThl4X-ksw3cuXvISlqUOY8GH54MvPs9mNDDyg2-i5mBsZhKZJIUkVVOLO1dCN7U-wuUwNgTrGCsAMYKYOwJ_vYE2yh9_zzhXvivmEj4OBEebGt2LzaGq9kiDlGeTHIberPdy5X_BVxkooDb6wsQi_nN7Jb8hG_ZH9NTshQ |
CitedBy_id | crossref_primary_10_3390_ijms21249363 crossref_primary_10_1128_JB_00429_10 crossref_primary_10_1111_j_1365_2958_2009_06834_x crossref_primary_10_1111_j_1751_7915_2009_00091_x crossref_primary_10_1111_1751_7915_12096 crossref_primary_10_1016_j_molstruc_2021_131108 crossref_primary_10_1038_srep01107 crossref_primary_10_3390_genes10050339 crossref_primary_10_1128_AEM_01846_09 crossref_primary_10_1038_s41598_020_77927_w crossref_primary_10_1128_AEM_00700_12 crossref_primary_10_1016_j_fob_2014_03_001 crossref_primary_10_1016_j_jbiosc_2011_10_021 crossref_primary_10_3390_molecules23071530 crossref_primary_10_1016_j_jbiosc_2013_01_007 |
Cites_doi | 10.1046/j.1365-2958.2000.02100.x 10.1128/AEM.71.4.1754-1764.2005 10.1093/emboj/20.1.1 10.1111/j.1462-2920.2004.00657.x 10.1128/AEM.71.12.7705-7715.2005 10.1016/S0021-9258(17)37154-5 10.1111/j.1462-2920.2004.00645.x 10.1099/mic.0.27217-0 10.1007/BF00122421 10.1128/JB.182.19.5448-5453.2000 10.1016/j.mib.2004.04.001 10.1007/s00253-007-0997-6 10.1073/pnas.82.4.1074 10.1016/0076-6879(94)35157-0 10.1046/j.1365-2672.1998.00525.x 10.1111/j.1349-7006.2000.tb00907.x 10.1128/JB.187.12.4050-4063.2005 10.1128/JB.185.6.2026-2030.2003 10.1271/bbb.68.787 10.1128/jb.174.9.2986-2992.1992 10.1093/nar/25.17.3389 10.1271/bbb.60663 10.1128/AEM.65.4.1806-1810.1999 10.1002/pmic.200500422 10.1007/BF00696222 10.1111/j.1365-2958.2007.05647.x 10.1016/S0022-2836(83)80284-8 10.1073/pnas.0607048103 10.1128/JB.01122-07 10.1007/BF00508122 10.1128/jb.179.8.2772-2776.1997 10.1007/BF00272133 10.1101/gr.9.1.27 10.1128/jb.178.23.6817-6823.1996 10.1128/AEM.68.10.4841-4846.2002 10.1128/JB.00057-07 10.1128/JB.182.3.789-795.2000 10.1128/JB.01443-07 10.1016/0003-2697(76)90527-3 10.1128/JB.186.7.2134-2146.2004 10.1128/JB.186.18.6101-6109.2004 10.1128/JB.187.13.4497-4504.2005 10.1016/S0378-1119(96)00748-2 10.1099/00221287-148-3-793 |
ContentType | Journal Article |
Copyright | 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd. Copyright John Wiley & Sons, Inc. Mar 2009 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd 2009 |
Copyright_xml | – notice: 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd – notice: 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd. – notice: Copyright John Wiley & Sons, Inc. Mar 2009 – notice: 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd 2009 |
DBID | BSCLL CGR CUY CVF ECM EIF NPM AAYXX CITATION 3V. 7QO 7T7 7X7 7XB 8FD 8FE 8FG 8FH 8FI 8FJ 8FK ABJCF ABUWG AFKRA AZQEC BBNVY BENPR BGLVJ BHPHI C1K CCPQU DWQXO FR3 FYUFA GHDGH GNUQQ HCIFZ K9. L6V LK8 M0S M7P M7S P64 PIMPY PQEST PQQKQ PQUKI PRINS PTHSS RC3 5PM |
DOI | 10.1111/j.1751-7915.2009.00086.x |
DatabaseName | Istex Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef ProQuest Central (Corporate) Biotechnology Research Abstracts Industrial and Applied Microbiology Abstracts (Microbiology A) Health & Medical Collection ProQuest Central (purchase pre-March 2016) Technology Research Database ProQuest SciTech Collection ProQuest Technology Collection ProQuest Natural Science Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) Materials Science & Engineering Collection ProQuest Central (Alumni) ProQuest Central ProQuest Central Essentials Biological Science Collection ProQuest Central Technology Collection 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 SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) ProQuest Engineering Collection Biological Sciences Health & Medical Collection (Alumni Edition) Biological Science Database Engineering Database Biotechnology and BioEngineering Abstracts Publicly Available Content Database ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China Engineering Collection Genetics Abstracts PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Publicly Available Content Database ProQuest Central Student Technology Collection Technology Research Database ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest Natural Science Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest Central Genetics Abstracts ProQuest Engineering Collection Health Research Premium Collection Biotechnology Research Abstracts Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Biological Science Collection Industrial and Applied Microbiology Abstracts (Microbiology A) Engineering Collection Engineering Database ProQuest Biological Science Collection ProQuest One Academic Eastern Edition ProQuest Hospital Collection ProQuest Technology 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 One Academic UKI Edition Materials Science & Engineering Collection Engineering Research Database ProQuest One Academic ProQuest Central (Alumni) |
DatabaseTitleList | MEDLINE CrossRef Publicly Available Content Database |
Database_xml | – sequence: 1 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: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: 8FG name: ProQuest Technology Collection url: https://search.proquest.com/technologycollection1 sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering |
EISSN | 1751-7915 |
EndPage | 273 |
ExternalDocumentID | 10_1111_j_1751_7915_2009_00086_x 21261920 MBT086 ark_67375_WNG_7TLRBW0V_K |
Genre | article Research Support, Non-U.S. Gov't Journal Article |
GeographicLocations | Japan |
GeographicLocations_xml | – name: Japan |
GroupedDBID | --- 0R~ 123 1OC 24P 29M 31~ 4.4 53G 5DZ 5VS 7X7 8-1 8FE 8FG 8FH 8FI 8FJ A8Z AAHHS AAZKR ABDBF ABJCF ABPTK ABUWG ACBWZ ACCFJ ACGFO ACIWK ACPRK ACXQS ADBBV ADKYN ADPDF ADRAZ ADZMN AEEZP AEGXH AENEX AEQDE AEUQT AFKRA AFRAH AHMBA AIAGR AIWBW AJBDE ALAGY ALMA_UNASSIGNED_HOLDINGS AOIJS ASPBG AVUZU AVWKF AZFZN BAWUL BBNVY BCNDV BDRZF BENPR BGLVJ BHPHI BPHCQ BSCLL BVXVI CAG CCPQU COF CS3 D-9 DIK EBD EBS EJD EMOBN ESTFP ESX F5P FEDTE FYUFA GODZA GROUPED_DOAJ GX1 HCIFZ HMCUK HVGLF HYE IAO IHR KQ8 L6V LH4 LK8 LW6 M48 M7P M7S ML0 MM. O9- OK1 OVD OVEED P2P PIMPY PQQKQ PROAC PTHSS RNS RPM SV3 TEORI TUS UKHRP WIN ALIPV ALUQN OIG CGR CUY CVF ECM EIF NPM AAYXX CITATION 3V. 7QO 7T7 7XB 8FD 8FK AZQEC C1K DWQXO FR3 GNUQQ K9. P64 PQEST PQUKI PRINS RC3 5PM |
ID | FETCH-LOGICAL-c6046-16f965017991994a04669449222753d47a29add8e788b2747669c164f42d13703 |
IEDL.DBID | RPM |
ISSN | 1751-7915 |
IngestDate | Tue Sep 17 21:28:53 EDT 2024 Fri Sep 13 06:44:36 EDT 2024 Fri Aug 23 00:40:13 EDT 2024 Thu May 23 23:17:20 EDT 2024 Sat Aug 24 00:59:37 EDT 2024 Wed Jan 17 05:01:23 EST 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 2 |
Language | English |
License | 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c6046-16f965017991994a04669449222753d47a29add8e788b2747669c164f42d13703 |
Notes | Supporting info itemSupporting info item istex:B48622A9C1862924FBE9956641B645184858D5B6 ark:/67375/WNG-7TLRBW0V-K ArticleID:MBT086 |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815846/ |
PMID | 21261920 |
PQID | 2299173905 |
PQPubID | 1016378 |
PageCount | 12 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_3815846 proquest_journals_2299173905 crossref_primary_10_1111_j_1751_7915_2009_00086_x pubmed_primary_21261920 wiley_primary_10_1111_j_1751_7915_2009_00086_x_MBT086 istex_primary_ark_67375_WNG_7TLRBW0V_K |
PublicationCentury | 2000 |
PublicationDate | March 2009 |
PublicationDateYYYYMMDD | 2009-03-01 |
PublicationDate_xml | – month: 03 year: 2009 text: March 2009 |
PublicationDecade | 2000 |
PublicationPlace | Oxford, UK |
PublicationPlace_xml | – name: Oxford, UK – name: United States – name: Bedford |
PublicationTitle | Microbial biotechnology |
PublicationTitleAlternate | Microbial Biotechnology |
PublicationYear | 2009 |
Publisher | Blackwell Publishing Ltd John Wiley & Sons, Inc |
Publisher_xml | – name: Blackwell Publishing Ltd – name: John Wiley & Sons, Inc |
References | König, C., Eulberg, D., Gröning, J., Lakner, S., Seibert, V., Kaschabek, S.R., and Schlömann, M. (2004) A linear megaplasmid, p1CP, carrying the genes for chlorocatechol catabolism of Rhodococcus opacus 1CP. Microbiology 150: 3075-3087. Takeda, H., Yamada, A., Miyauchi, K., Masai, E., and Fukuda, M. (2004) Characterization of transcriptional regulatory genes for biphenyl degradation in Rhodococcus sp. strain RHA1. J Bacteriol 186: 2134-2146. Iwasaki, T., Takeda, H., Miyauchi, K., Yamada, T., Masai, E., and Fukuda, M. (2007) Characterization of two biphenyl dioxygenases for biphenyl/PCB degradation in a PCB degrader, Rhodococcus sp. strain RHA1. Biosci Biotechnol Biochem 71: 993-1002. Hernáez, M.J., Floriano, B., Ríos, J.J., and Santero, E. (2002) Identification of a hydratase and a class II aldolase involved in biodegradation of the organic solvent tetralin. Appl Environ Microbiol 68: 4841-4846. Nagy, I., Verheijen, S., De Schrijver, A., Van Damme, J., Proost, P., Schoofs, G., et al. (1995) Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol: N,N'-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides. Arch Microbiol 163: 439-446. Labbé, D., Garnon, J., and Lau, P.C. (1997) Characterization of the genes encoding a receptor-like histidine kinase and a cognate response regulator from a biphenyl/polychlorobiphenyl-degrading bacterium, Rhodococcus sp. strain M5. J Bacteriol 179: 2772-2776. Hugenholtz, P., Pitulle, C., Hershberger, K.L., and Pace, N.R. (1998) Novel division level bacterial diversity in a Yellowstone hot spring. J Bacteriol 180: 366-376. Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557-580. Sikkema, J., De Bont, J.A.M., and Poolman, B. (1994) Interactions of cyclic hydrocarbons with biological membranes. J Biol Chem 269: 8022-8028. Dorn, E., Hellwig, M., Reineke, W., and Knackmuss, H.J. (1974) Isolation and characterization of a 3-chlorobenzoate degrading. Pseudomonas. Arch Microbiol 99: 61-70. Neuwald, A.F., Aravind, L., Spouge, J.L., and Koonin, E.V. (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27-43. Hernáez, M.J., Reineke, W., and Santero, E. (1999) Genetic analysis of biodegradation of tetralin by a Sphingomonas strain. Appl Environ Microbiol 65: 1806-1810. Schreiber, A.F., and Winkler, U.K. (1983) Transformation of tetralin by whole cells of Pseudomonas stutzeri AS39. J Appl Microbiol Biotechnol 18: 6-10. White, C.E., and Winans, S.C. (2007) The quorum-sensing transcription factor TraR decodes its DNA binding site by direct contacts with DNA bases and by detection of DNA flexibility. Mol Microbiol 64: 245-256. Hernáez, M.J., Andújar, E., Ríos, J.L., Kaschabek, S.R., Reineke, W., and Santero, E. (2000) Identification of a serine hydrolase which cleaves the alicyclic ring of tetralin. J Bacteriol 182: 5448-5453. Kim, D., Chae, J.C., Zylstra, G.J., Sohn, H.Y., Kwon, G.S., and Kim, E. (2005) Identification of two-component regulatory genes involved in o-xylene degradation by Rhodococcus sp. strain DK17. J Microbiol 43: 49-53. McLeod, M.P., Warren, R.L., Hsiao, W.W.L., Araki, N., Myhre, M., Fernandes, C., et al. (2006) The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse. Proc Natl Acad Sci USA 103: 15582-15587. Moreno-Ruiz, E., Hernáez, M.J., Martínez-Pérez, O., and Santero, E. (2003) Identification and functional characterization of Sphingomonas macrogolitabida strain TFA genes involved in the first two steps of the tetralin catabolic pathway. J Bacteriol 185: 2026-2030. Navarro-Llorens, J.M., Patrauchan, M.A., Stewart, J.R., Davies, J.E., Eltis, L.D., and Mohn, W.W. (2005) Phenylacetate catabolism in Rhodococcus sp. strain RHA1: a central pathway for degradation of aromatic compounds. J Bacteriol 187: 4497-4504. Tabor, S., and Richardson, C.C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci USA 82: 1074-1078. Govantes, F., Albrecht, J.A., and Gunsalus, R.P. (2000) Oxygen regulation of the Escherichia coli cytochrome d oxidase cydAB operon: roles of multiple promoters and the Fnr-1 and Fnr-2 binding sites. Mol Microbiol 6: 1456-1469. Govantes, F., Molina-López, J.A., and Santero, E. (1996) Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae. J Bacteriol 178: 6817-6823. Kulakov, L.A., Chen, S., Allen, C.C., and Larkin, M.J. (2005) Web-type evolution of rhodococcus gene clusters associated with utilization of naphthalene. Appl Environ Microbiol 71: 1754-1764. Veselý, M., Knoppová, M., Nesvera, J., and Pátek, M. (2007) Analysis of catRABC operon for catechol degradation from phenol-degrading Rhodococcus erythropolis. Appl Microbiol Biotechnol 76: 159-168. Van Der Geize, R., and Dijkhuizen, L. (2004) Harnessing the catabolic diversity of rhodococci for environmental and biotechnological applications. Curr Opin Microbiol 7: 255-261. Maruyama, T., Ishikura, M., Taki, H., Shindo, K., Kasai, H., Haga, M., et al. (2005) Isolation and characterization of o-xylene oxygenase genes from Rhodococcus opacus TKN14. Appl Environ Microbiol 71: 7705-7715. Masai, E., Sugiyama, K., Iwashita, N., Shimizu, S., Hauschild, J.E., Hatta, T., et al. (1997) The bphDEF meta-cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in Rhodococcus sp. strain RHA1. Gene 187: 141-149. Bell, K.S., Philip, J.C., Aw, D.W.J., and Christoff, N. (1998) The genus. Rhodococcus. J Appl Microbiol 85: 195-210. Martínez-Pérez, O., Moreno-Ruiz, E., Floriano, B., and Santero, E. (2004) Regulation of tetralin biodegradation and identification of genes essential for expression of thn operons. J Bacteriol 186: 6101-6109. De Lorenzo, V., and Timmis, K.N. (1994) Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons. Methods Enzymol 235: 386-405. Cormack, B.P., Valdivia, R.H., and Falkow, S. (1996) FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173: 33-38. Sikkema, J., and De Bont, J.A.M. (1991) Isolation and initial characterization of bacteria growing on tetralin. Biodegradation 2: 15-23. Tomás-Gallardo, L., Canosa, I., Santero, E., Camafeita, E., Calvo, E., López, J.A., and Floriano, B. (2006) Proteomic and transcriptional characterization of aromatic degradation pathways in Rhodoccocus sp. strain TFB. Proteomics 6: 119-132. Kelly, B.G., Wall, D.M., Boland, C.A., and Meijer, W.G. (2002) Isocitrate lyase of the facultative intracellular pathogen Rhodococcus equi. Microbiology 148: 793-798. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254. Cases, I., and De Lorenzo, V. (2001) The black cat/white cat principle of signal integration in bacterial promoters. EMBO J 20: 1-11. Taguchi, K., Motoyama, M., and Kudo, T. (2004) Multiplicity of 2,3-dihydroxybiphenyl dioxygenase genes in the Gram-positive polychlorinated biphenyl degrading bacterium Rhodococcus rhodochrous K37. Biosci Biotechnol Biochem 68: 787-795. Martínez-Pérez, O., López-Sánchez, A., Reyes-Ramírez, F., Floriano, B., and Santero, E. (2007) Integrated response to inducers by communication between a catabolic pathway and its regulatory system. J Bacteriol 189: 3768-3775. Sambrook, J., Fritsch, E.F., and Winkler, U.K. (1989) Molecular Cloning: A Laboratory Manual, 2nd, edn. Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory. Altschul, S.F., Madden, T.L., Schäffer, A.A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402. Antunes, L.C., Ferreira, R.B., Lostroh, C.P., and Greenberg, E.P. (2008) A mutational analysis defines Vibrio fischeri LuxR binding sites. J Bacteriol 190: 4392-4397. Patrauchan, M.A., Florizone, C., Eapen, S., Gómez-Gil, L., Sethuraman, B., Fukuda, M., et al. (2008) Roles of ring-hydroxylating dioxygenases in styrene and benzene catabolism in Rhodococcus jostii RHA1. J Bacteriol 190: 37-47. Sikkema, J., Poolman, B., Konings, W.N., and De Bont, J.A.M. (1992) Effects of the membrane action of tetralin on the functional and structural properties of artificial and bacterial membranes. J Bacteriol 174: 2986-2992. Tropel, D., Bähler, A., Globig, K., and Van Der Meer, J.R. (2004) Design of new promoters and of a dual-bioreporter based on cross-activation by the two regulatory proteins XylR and HbpR. Environ Microbiol 6: 1186-1196. Patrauchan, M.A., Florizone, C., Dosanjh, M., William W., Mohn, W.W., Davies, J., and Eltis, L.D. (2005) Catabolism of benzoate and phthalate in Rhodococcus sp. strain RHA1: redundancies and convergence. J. Bacteriol 187: 4050-4063. Andújar, E., Hernáez, M.J., Kaschabek, S.R., Reineke, W., and Santero, E. (2000) Identification of an extradiol dioxygenase involved in tetralin biodegradation: gene sequence analysis and purification and characterization of the gene product. J Bacteriol 182: 789-795. 1998; 180 1997; 179 2008; 190 2007; 189 1991; 2 2004; 186 1974; 99 1994; 235 2000; 6 1997; 25 2004; 7 2004; 68 2004; 6 1999; 65 2005; 43 2006; 6 2007; 71 1985; 82 1998; 85 1983; 18 2007; 76 2001; 20 1999; 9 1983; 166 1994; 269 2005; 187 1992; 174 1976; 72 2002; 68 1997; 187 2004; 150 2000; 182 1996; 173 2002; 148 2005; 71 2007; 64 1996; 178 1995; 163 2006; 103 1989 2003; 185 15479251 - Environ Microbiol. 2004 Nov;6(11):1186-96 17483937 - Appl Microbiol Biotechnol. 2007 Aug;76(1):159-68 18083819 - J Bacteriol. 2008 Jul;190(13):4392-7 6345791 - J Mol Biol. 1983 Jun 5;166(4):557-80 15118304 - Biosci Biotechnol Biochem. 2004 Apr;68(4):787-95 11882714 - Microbiology. 2002 Mar;148(Pt 3):793-8 9927482 - Genome Res. 1999 Jan;9(1):27-43 8132524 - J Biol Chem. 1994 Mar 18;269(11):8022-8 17965160 - J Bacteriol. 2008 Jan;190(1):37-47 9073078 - Gene. 1997 Mar 10;187(1):141-9 942051 - Anal Biochem. 1976 May 7;72:248-54 15342579 - J Bacteriol. 2004 Sep;186(18):6101-9 17351041 - J Bacteriol. 2007 May;189(10):3768-75 15937168 - J Bacteriol. 2005 Jun;187(12):4050-63 10633115 - J Bacteriol. 2000 Feb;182(3):789-95 9254694 - Nucleic Acids Res. 1997 Sep 1;25(17):3389-402 9440526 - J Bacteriol. 1998 Jan;180(2):366-76 15811998 - Appl Environ Microbiol. 2005 Apr;71(4):1754-64 15347765 - Microbiology. 2004 Sep;150(Pt 9):3075-87 4852581 - Arch Microbiol. 1974;99(1):61-70 3156376 - Proc Natl Acad Sci U S A. 1985 Feb;82(4):1074-8 10998176 - Mol Microbiol. 2000 Sep;37(6):1456-69 16332743 - Appl Environ Microbiol. 2005 Dec;71(12):7705-15 16544280 - Proteomics. 2006 Apr;6 Suppl 1:S119-32 17420585 - Biosci Biotechnol Biochem. 2007 Apr;71(4):993-1002 17030794 - Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15582-7 17376086 - Mol Microbiol. 2007 Apr;64(1):245-56 15196492 - Curr Opin Microbiol. 2004 Jun;7(3):255-61 15028699 - J Bacteriol. 2004 Apr;186(7):2134-46 1314806 - J Bacteriol. 1992 May;174(9):2986-92 10103288 - Appl Environ Microbiol. 1999 Apr;65(4):1806-10 15968060 - J Bacteriol. 2005 Jul;187(13):4497-504 9098081 - J Bacteriol. 1997 Apr;179(8):2772-6 8955302 - J Bacteriol. 1996 Dec;178(23):6817-23 8057911 - Methods Enzymol. 1994;235:386-405 8707053 - Gene. 1996;173(1 Spec No):33-8 12618469 - J Bacteriol. 2003 Mar;185(6):2026-30 9750292 - J Appl Microbiol. 1998 Aug;85(2):195-210 12324329 - Appl Environ Microbiol. 2002 Oct;68(10):4841-6 7575099 - Arch Microbiol. 1995 Jun;163(6):439-46 10986248 - J Bacteriol. 2000 Oct;182(19):5448-53 11226149 - EMBO J. 2001 Jan 15;20(1-2):1-11 15765058 - J Microbiol. 2005 Feb;43(1):49-53 e_1_2_6_32_1 Sambrook J. (e_1_2_6_36_1) 1989 e_1_2_6_10_1 e_1_2_6_31_1 e_1_2_6_30_1 Kim D. (e_1_2_6_20_1) 2005; 43 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_35_1 e_1_2_6_11_1 e_1_2_6_34_1 e_1_2_6_12_1 e_1_2_6_33_1 e_1_2_6_17_1 e_1_2_6_18_1 e_1_2_6_39_1 e_1_2_6_15_1 e_1_2_6_38_1 e_1_2_6_16_1 e_1_2_6_37_1 e_1_2_6_42_1 e_1_2_6_43_1 e_1_2_6_21_1 e_1_2_6_41_1 e_1_2_6_40_1 e_1_2_6_9_1 e_1_2_6_8_1 e_1_2_6_5_1 e_1_2_6_4_1 e_1_2_6_7_1 e_1_2_6_6_1 Hernáez M.J. (e_1_2_6_14_1) 1999; 65 e_1_2_6_25_1 e_1_2_6_24_1 e_1_2_6_3_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_22_1 e_1_2_6_29_1 e_1_2_6_44_1 e_1_2_6_28_1 e_1_2_6_45_1 e_1_2_6_27_1 e_1_2_6_46_1 e_1_2_6_26_1 e_1_2_6_47_1 |
References_xml | – volume: 6 start-page: 1456 year: 2000 end-page: 1469 article-title: Oxygen regulation of the cytochrome d oxidase operon: roles of multiple promoters and the Fnr‐1 and Fnr‐2 binding sites publication-title: Mol Microbiol – volume: 18 start-page: 6 year: 1983 end-page: 10 article-title: Transformation of tetralin by whole cells of Pseudomonas stutzeri AS39 publication-title: J Appl Microbiol Biotechnol – volume: 190 start-page: 4392 year: 2008 end-page: 4397 article-title: A mutational analysis defines LuxR binding sites publication-title: J Bacteriol – volume: 148 start-page: 793 year: 2002 end-page: 798 article-title: Isocitrate lyase of the facultative intracellular pathogen equi publication-title: Microbiology – volume: 71 start-page: 1754 year: 2005 end-page: 1764 article-title: Web‐type evolution of rhodococcus gene clusters associated with utilization of naphthalene publication-title: Appl Environ Microbiol – volume: 7 start-page: 255 year: 2004 end-page: 261 article-title: Harnessing the catabolic diversity of rhodococci for environmental and biotechnological applications publication-title: Curr Opin Microbiol – volume: 179 start-page: 2772 year: 1997 end-page: 2776 article-title: Characterization of the genes encoding a receptor‐like histidine kinase and a cognate response regulator from a biphenyl/polychlorobiphenyl‐degrading bacterium, Rhodococcus sp. strain M5 publication-title: J Bacteriol – volume: 235 start-page: 386 year: 1994 end-page: 405 article-title: Analysis and construction of stable phenotypes in gram‐negative bacteria with Tn5‐ and Tn10‐derived minitransposons publication-title: Methods Enzymol – volume: 71 start-page: 7705 year: 2005 end-page: 7715 article-title: Isolation and characterization of o‐xylene oxygenase genes from Rhodococcus opacus TKN14 publication-title: Appl Environ Microbiol – volume: 187 start-page: 4497 year: 2005 end-page: 4504 article-title: Phenylacetate catabolism in sp. strain RHA1: a central pathway for degradation of aromatic compounds publication-title: J Bacteriol – year: 1989 – volume: 99 start-page: 61 year: 1974 end-page: 70 article-title: Isolation and characterization of a 3‐chlorobenzoate degrading publication-title: Pseudomonas. Arch Microbiol – volume: 6 start-page: 119 year: 2006 end-page: 132 article-title: Proteomic and transcriptional characterization of aromatic degradation pathways in Rhodoccocus sp. strain TFB publication-title: Proteomics – volume: 178 start-page: 6817 year: 1996 end-page: 6823 article-title: Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae publication-title: J Bacteriol – volume: 65 start-page: 1806 year: 1999 end-page: 1810 article-title: Genetic analysis of biodegradation of tetralin by a Sphingomonas strain publication-title: Appl Environ Microbiol – volume: 6 start-page: 1186 year: 2004 end-page: 1196 article-title: Design of new promoters and of a dual‐bioreporter based on cross‐activation by the two regulatory proteins XylR and HbpR publication-title: Environ Microbiol – volume: 76 start-page: 159 year: 2007 end-page: 168 article-title: Analysis of catRABC operon for catechol degradation from phenol‐degrading publication-title: Appl Microbiol Biotechnol – volume: 180 start-page: 366 year: 1998 end-page: 376 article-title: Novel division level bacterial diversity in a Yellowstone hot spring publication-title: J Bacteriol – volume: 186 start-page: 6101 year: 2004 end-page: 6109 article-title: Regulation of tetralin biodegradation and identification of genes essential for expression of operons publication-title: J Bacteriol – volume: 25 start-page: 3389 year: 1997 end-page: 3402 article-title: Gapped BLAST and PSI‐BLAST: a new generation of protein database search programs publication-title: Nucleic Acids Res – volume: 43 start-page: 49 year: 2005 end-page: 53 article-title: Identification of two‐component regulatory genes involved in o‐xylene degradation by Rhodococcus sp. strain DK17 publication-title: J Microbiol – volume: 82 start-page: 1074 year: 1985 end-page: 1078 article-title: A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes publication-title: Proc Natl Acad Sci USA – volume: 64 start-page: 245 year: 2007 end-page: 256 article-title: The quorum‐sensing transcription factor TraR decodes its DNA binding site by direct contacts with DNA bases and by detection of DNA flexibility publication-title: Mol Microbiol – volume: 186 start-page: 2134 year: 2004 end-page: 2146 article-title: Characterization of transcriptional regulatory genes for biphenyl degradation in sp. strain RHA1 publication-title: J Bacteriol – volume: 166 start-page: 557 year: 1983 end-page: 580 article-title: Studies on transformation of with plasmids publication-title: J Mol Biol – volume: 182 start-page: 5448 year: 2000 end-page: 5453 article-title: Identification of a serine hydrolase which cleaves the alicyclic ring of tetralin publication-title: J Bacteriol – volume: 68 start-page: 4841 year: 2002 end-page: 4846 article-title: Identification of a hydratase and a class II aldolase involved in biodegradation of the organic solvent tetralin publication-title: Appl Environ Microbiol – volume: 187 start-page: 4050 year: 2005 end-page: 4063 article-title: Catabolism of benzoate and phthalate in Rhodococcus sp. strain RHA1: redundancies and convergence publication-title: J. Bacteriol – volume: 68 start-page: 787 year: 2004 end-page: 795 article-title: Multiplicity of 2,3‐dihydroxybiphenyl dioxygenase genes in the Gram‐positive polychlorinated biphenyl degrading bacterium K37 publication-title: Biosci Biotechnol Biochem – volume: 174 start-page: 2986 year: 1992 end-page: 2992 article-title: Effects of the membrane action of tetralin on the functional and structural properties of artificial and bacterial membranes publication-title: J Bacteriol – volume: 182 start-page: 789 year: 2000 end-page: 795 article-title: Identification of an extradiol dioxygenase involved in tetralin biodegradation: gene sequence analysis and purification and characterization of the gene product publication-title: J Bacteriol – volume: 20 start-page: 1 year: 2001 end-page: 11 article-title: The black cat/white cat principle of signal integration in bacterial promoters publication-title: EMBO J – volume: 269 start-page: 8022 year: 1994 end-page: 8028 article-title: Interactions of cyclic hydrocarbons with biological membranes publication-title: J Biol Chem – volume: 2 start-page: 15 year: 1991 end-page: 23 article-title: Isolation and initial characterization of bacteria growing on tetralin publication-title: Biodegradation – volume: 103 start-page: 15582 year: 2006 end-page: 15587 article-title: The complete genome of sp. RHA1 provides insights into a catabolic powerhouse publication-title: Proc Natl Acad Sci USA – volume: 187 start-page: 141 year: 1997 end-page: 149 article-title: The bphDEF meta‐cleavage pathway genes involved in biphenyl/polychlorinated biphenyl degradation are located on a linear plasmid and separated from the initial bphACB genes in sp. strain RHA1 publication-title: Gene – volume: 9 start-page: 27 year: 1999 end-page: 43 article-title: AAA+: a class of chaperone‐like ATPases associated with the assembly, operation, and disassembly of protein complexes publication-title: Genome Res – volume: 71 start-page: 993 year: 2007 end-page: 1002 article-title: Characterization of two biphenyl dioxygenases for biphenyl/PCB degradation in a PCB degrader, sp. strain RHA1 publication-title: Biosci Biotechnol Biochem – volume: 185 start-page: 2026 year: 2003 end-page: 2030 article-title: Identification and functional characterization of strain TFA genes involved in the first two steps of the tetralin catabolic pathway publication-title: J Bacteriol – volume: 189 start-page: 3768 year: 2007 end-page: 3775 article-title: Integrated response to inducers by communication between a catabolic pathway and its regulatory system publication-title: J Bacteriol – volume: 150 start-page: 3075 year: 2004 end-page: 3087 article-title: A linear megaplasmid, p1CP, carrying the genes for chlorocatechol catabolism of 1CP publication-title: Microbiology – volume: 72 start-page: 248 year: 1976 end-page: 254 article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein‐dye binding publication-title: Anal Biochem – volume: 173 start-page: 33 year: 1996 end-page: 38 article-title: FACS‐optimized mutants of the green fluorescent protein (GFP) publication-title: Gene – volume: 163 start-page: 439 year: 1995 end-page: 446 article-title: Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol: N,N'‐dimethyl‐4‐nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides publication-title: Arch Microbiol – volume: 190 start-page: 37 year: 2008 end-page: 47 article-title: Roles of ring‐hydroxylating dioxygenases in styrene and benzene catabolism in jostii RHA1 publication-title: J Bacteriol – volume: 85 start-page: 195 year: 1998 end-page: 210 article-title: The genus publication-title: Rhodococcus. J Appl Microbiol – ident: e_1_2_6_12_1 doi: 10.1046/j.1365-2958.2000.02100.x – ident: e_1_2_6_21_1 doi: 10.1128/AEM.71.4.1754-1764.2005 – ident: e_1_2_6_7_1 doi: 10.1093/emboj/20.1.1 – ident: e_1_2_6_17_1 doi: 10.1111/j.1462-2920.2004.00657.x – ident: e_1_2_6_28_1 doi: 10.1128/AEM.71.12.7705-7715.2005 – ident: e_1_2_6_40_1 doi: 10.1016/S0021-9258(17)37154-5 – ident: e_1_2_6_45_1 doi: 10.1111/j.1462-2920.2004.00645.x – ident: e_1_2_6_22_1 doi: 10.1099/mic.0.27217-0 – ident: e_1_2_6_38_1 doi: 10.1007/BF00122421 – ident: e_1_2_6_15_1 doi: 10.1128/JB.182.19.5448-5453.2000 – ident: e_1_2_6_10_1 doi: 10.1016/j.mib.2004.04.001 – ident: e_1_2_6_46_1 doi: 10.1007/s00253-007-0997-6 – ident: e_1_2_6_41_1 doi: 10.1073/pnas.82.4.1074 – ident: e_1_2_6_24_1 doi: 10.1016/0076-6879(94)35157-0 – ident: e_1_2_6_5_1 doi: 10.1046/j.1365-2672.1998.00525.x – ident: e_1_2_6_8_1 doi: 10.1111/j.1349-7006.2000.tb00907.x – ident: e_1_2_6_34_1 doi: 10.1128/JB.187.12.4050-4063.2005 – ident: e_1_2_6_30_1 doi: 10.1128/JB.185.6.2026-2030.2003 – volume-title: Molecular Cloning: A Laboratory Manual year: 1989 ident: e_1_2_6_36_1 contributor: fullname: Sambrook J. – ident: e_1_2_6_42_1 doi: 10.1271/bbb.68.787 – ident: e_1_2_6_39_1 doi: 10.1128/jb.174.9.2986-2992.1992 – ident: e_1_2_6_2_1 doi: 10.1093/nar/25.17.3389 – ident: e_1_2_6_18_1 doi: 10.1271/bbb.60663 – volume: 65 start-page: 1806 year: 1999 ident: e_1_2_6_14_1 article-title: Genetic analysis of biodegradation of tetralin by a Sphingomonas strain publication-title: Appl Environ Microbiol doi: 10.1128/AEM.65.4.1806-1810.1999 contributor: fullname: Hernáez M.J. – ident: e_1_2_6_44_1 doi: 10.1002/pmic.200500422 – ident: e_1_2_6_9_1 doi: 10.1007/BF00696222 – ident: e_1_2_6_47_1 doi: 10.1111/j.1365-2958.2007.05647.x – ident: e_1_2_6_13_1 doi: 10.1016/S0022-2836(83)80284-8 – ident: e_1_2_6_25_1 doi: 10.1073/pnas.0607048103 – ident: e_1_2_6_35_1 doi: 10.1128/JB.01122-07 – ident: e_1_2_6_37_1 doi: 10.1007/BF00508122 – ident: e_1_2_6_23_1 doi: 10.1128/jb.179.8.2772-2776.1997 – ident: e_1_2_6_31_1 doi: 10.1007/BF00272133 – ident: e_1_2_6_33_1 doi: 10.1101/gr.9.1.27 – ident: e_1_2_6_11_1 doi: 10.1128/jb.178.23.6817-6823.1996 – ident: e_1_2_6_16_1 doi: 10.1128/AEM.68.10.4841-4846.2002 – ident: e_1_2_6_27_1 doi: 10.1128/JB.00057-07 – ident: e_1_2_6_3_1 doi: 10.1128/JB.182.3.789-795.2000 – ident: e_1_2_6_4_1 doi: 10.1128/JB.01443-07 – ident: e_1_2_6_6_1 doi: 10.1016/0003-2697(76)90527-3 – volume: 43 start-page: 49 year: 2005 ident: e_1_2_6_20_1 article-title: Identification of two‐component regulatory genes involved in o‐xylene degradation by Rhodococcus sp. strain DK17 publication-title: J Microbiol contributor: fullname: Kim D. – ident: e_1_2_6_43_1 doi: 10.1128/JB.186.7.2134-2146.2004 – ident: e_1_2_6_26_1 doi: 10.1128/JB.186.18.6101-6109.2004 – ident: e_1_2_6_32_1 doi: 10.1128/JB.187.13.4497-4504.2005 – ident: e_1_2_6_29_1 doi: 10.1016/S0378-1119(96)00748-2 – ident: e_1_2_6_19_1 doi: 10.1099/00221287-148-3-793 |
SSID | ssj0060052 |
Score | 1.9515209 |
Snippet | Summary
The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using... The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram-positive bacterium resistant to genetic manipulation, was characterized using a... Summary The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using... The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a... The tetralin biodegradation pathway in Rhodococcus sp. strain TFB, a Gram‐positive bacterium resistant to genetic manipulation, was characterized using a... |
SourceID | pubmedcentral proquest crossref pubmed wiley istex |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 262 |
SubjectTerms | Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Biodegradation Biodegradation, Environmental Carbon Catabolite repression Cloning Dehydrogenases Electrophoresis, Gel, Two-Dimensional Gene expression Gene Expression Regulation, Bacterial Genes Genetic engineering Genetics Genomes Glucose Mass spectrometry Metabolic Networks and Pathways Metabolism Molecular Sequence Data Mutation Nucleotides Operon Operons Plasmids Promoter Regions, Genetic Proteins Proteomics Regulatory sequences Rhodococcus Rhodococcus - chemistry Rhodococcus - genetics Rhodococcus - metabolism Scientific imaging Tetrahydronaphthalenes - metabolism Tetralin Transcription |
SummonAdditionalLinks | – databaseName: Health & Medical Collection dbid: 7X7 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3JTsMwEB0VuMABsRMoyAfELbROkzg-IYooFVAOqEBvVpxFIFBaaBHw98w4C2UR4hJF2ZTkOeP3nPEbgD3yDIu0duxmwls2OXDZgcRF7IS-CJ1UBy2aO9y79LvX7tnAG9SgW86FobTKMiaaQB0PIxojbzgYN7lAhe41Qk2jANGkcTh6sql-FP1nLYppzMAcd5BWYMsWg0p6-TT6-S2Px-Nk1eiVlpVI7Uv7o6JzmqP3_PYb8_yZQDlNbE3P1FmCxYJSsqO8DSxDLclWYGHKaHAVHntlFVwWZjHT91QnyxgFsKhybM4nZLJhypAUsklixkAyFpOdRF55iVH94tfwneHmqzsUtBhNo5cxG48O2NgUm2D9TnsNrjsn_eOuXdRZsCMf5bHN_VQiUSNvOHIKDnGbL11X0jRZrxW7iJnEMBgkKJc1qVjcHaHMSl0n5i0MGeswmw2zZBOY5NpNYh77Ugs35TKIROqGAi9Ln3vQtICXL1iNcjsNNSVDEBRFoFBxTKkMKOrNgn2DRHVC-PxA6WjCU7eXp0r0L67at80bdW5BvYRKFV_iWH22Gws2ctSqC2G3TfoR70p8wbM6gLy3v-7J7u-MBzcSHaJuFngG-X8_jOq1-7iy9fetbsN8_teKct3qMDt5fkl2kPxM9K5p1x-YTf6u priority: 102 providerName: ProQuest – databaseName: Scholars Portal Open Access Journals dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8NAEB5EL3oQ38YXexBvKdlk89iDiBWrqO2htOptyZMWS9S2Yv33zmya0GoP4iWEPDYk32b2m92ZbwBOSTMsjiLbtFLumKTAZQYSN4kden5oZ1HgUO5ws-XddsXds_u8BGW64vQDjha6dlRPqjsc1CbvXxf4w5_PRuW4nIQX3VKAEol6DZnlii0cQf2-Kaq1BY9mQnWa5PSeH_E9i1rSksHa17Dmxq8VgmKyiJz-jrGc5b568GpswPqUdbLLoptswlKab8HajBbhNgyaZaFcFuYJi_pUSktrCbC4EnUucjbZa8aQN7JxqqdJcpaQ4kRRnIlRiePP8Ivh4XYPfV40uPHHiI3eamyk61GwTqO-A93Gdefq1pyWYjBjDz1ok3uZRC5H8nEkJhziMU8KISmT1nUSgbBKtJRBih51RI4uno7RE8uEnXAHrcouLOeveboPTPJIpAlPPBn5IuMyiP1MhD42SxYhsAzg5QdWb4XihprxVBAfRfhQ_UypND5qYsCZRqK6IRy-UMSa76qn1o3yOw_t-pP1qO4NOCqhUmVfUzYOydx3pOUasFegVjVUwm6AP4dndQHJc8-fyfs9LdONXIjYnQGuRv7PL6Oa9Q7uHPz7iYewWqx5UaTcESyPhx_pMVKncXSi_4RvIuwOvw priority: 102 providerName: Scholars Portal – databaseName: Wiley Open Access Journals dbid: 24P link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT8JAEN4YuejB-LaKZg_GWw3bbrvdoxiRqBhDQLltun1EoinGQsR_78z2EVAPxgshLbuBfjuz3ywz3xByipphkdaO3UqYa6MClx1IeImd0Behk-rAxdrh3r3fHfKbkTcq85-wFqbQh6gP3NAyjL9GAw91vmzkwmMot-hVspNAz8-BTzaA5QS4wh3-UHllH88_TXFkOeZbVs9vMy1tVQ186vPfeOjPdMpFmmv2qc4m2SgJJr0oVsQWWUmybbK-IDu4Q157VU9cGmYx1WPsmmVkA2hU6zcX5Zl0klKgiHSamBORjMYoLlH0YaLYzfgj_KRwuf8M4S341miW0_ztnOam9QQddNq7ZNi5Glx27bLrgh35ECzbzE8l0DZUikPd4BCu-ZJziUWznhtzQFCCUwwSCJ41xrRwO4KgK-VOzFxwIHtkNZtkyQGhkmmexCz2pRY8ZTKIRMpDAdOi8Qcti7DqAau3QlxDLQQlAIpCULBVplQGFDW3yJlBoh4Qvr9gcprw1NP9tRKDu377qfWobi3SrKBSpV3myoHdlwlXtjyL7Beo1RPBJo7RJHwrsYRn_QFU4l6-k42fjSI30B4kchbxDPJ__jGq1x7Am8N_jjsia8WfW5gS1ySr0_dZcgwcaapPzOL_AglNAv0 priority: 102 providerName: Wiley-Blackwell |
Title | Molecular and biochemical characterization of the tetralin degradation pathway in Rhodococcus sp. strain TFB |
URI | https://api.istex.fr/ark:/67375/WNG-7TLRBW0V-K/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1751-7915.2009.00086.x https://www.ncbi.nlm.nih.gov/pubmed/21261920 https://www.proquest.com/docview/2299173905/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC3815846 |
Volume | 2 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9tAEB4RuLSHqqW0uKXRHhA3J1577fUeG0RALY6iKJTcVl4_RASYiASV_vvOrO0oaTlUvazstb1-fN552DPfABwTZ1hmjO96BQ9cYuByY4VN7qeRTP3SxAHlDiej6OJKfJuFsx0I21wYG7SfmXmvurvvVfMbG1u5uM_6bZxYf5ycopYhvdnvQEcGQeui1-I3og-dNgsy5MTFGP4RvtP0tkyVaNFbLmqU4ORKeFvqaY-e9PNLtuffIZSbpq3VTcO38KYxKtnX-uLfwU5R7cPrDarB93CXtHVwWVrlzMypUpalCmDZmrO5TslkDyVDs5CtCvsVpGI5EUrUtZcYVTD-mf5i2D25QZcW5Wn2tGTLRY8tbbkJNh0ODuBqeDY9vXCbSgtuFqGD7PKoVGiqETsccQWn2BcpIRQlyoZBLhA1hYIwLtBhNuTH4uYMHa1S-DkPUGh8gN3qoSoOgSluRJHzPFJGipKrOJOlSCUOSxM-9hzg7QPWi5pQQ284IoiPJnyoPKbSFh_97MCJRWJ9QPp4SwFpMtTXo3Mtp5eTwbX3Q3934KiFSjdzcal91LhcBsoLHfhYo7YeqIXdAbmF53oHYt_e3oIvpWXhbl5CB0KL_D_fjE4GU1z49N9n_Ayv6l9aFAh3BLurx6fiC1pGK9OFji_G2MqZxDYenndhb3A2Gk9wLRFx186U3xWXCuc |
link.rule.ids | 230,315,733,786,790,891,2236,11589,12083,12792,21416,24346,27957,27958,31754,33408,33779,43345,43635,43840,46087,46511,50849,50958,53827,53829,74102,74392,74659 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1LT9tAEB5ROLQcEPQB5tU9IG5us_ba6z0hggihJDkgU3Jb-SkQyAk4CPj3zKwfDaVCvViWX1r7s2e_bz37DcAeeYYlcezYnYy7Njlw2YHCRepEvoycPA5cmjs8HPn9C_Fr7I3rAbeyTqtsYqIJ1OkkoTHynw7GTS5RoXsH0zubqkbR39W6hMYHWBKuKyilT45bweXTmOdf2TseJ4NGrzGqRELfmB7VXdISPd2nf_HNt2mT83TW9Ee9VVipiSQ7rJBfg4Ws-AzLc_aCX-B22NS-ZVGRsviaqmMZewCWtD7N1TRMNskZUkE2y8zIR8FSMpGo6i0xqlr8GD0z3Hx-hTIWY2jyULJy-oOVpsQEC3vdr3DROw6P-nZdXcFOfBTFNvdzhfSMHOHIHzjCbb4SQtHkWM9NBSKlMPgFGYrkmLQr7k5QXOXCSbmLgeIbLBaTItsApngsspSnvoqlyLkKEpmLSOJl6SMPOhbw5gHraWWioefEB4KiCRQqiam0AUU_WbBvkGhPiO5vKAlNevpydKJlODjvXnZ-6zMLthuodP39lfrP22LBeoVaeyHsrEk1YqvkKzzbA8hx-_We4vrKOG8jvSHCZoFnkP_vm9HDbogrm-839Tt87IfDgR6cjs624FP134qy3bZhcXb_kO0g_ZnFu-YdfwFOp_3h |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1LT9tAEB4VIlVwqPrg4UJhD4ibIeusvd5TRVoCFBKhKDxuKz8VROWkOKjw75lZr0N4CHGJIjuxbH_j2W_Ws98HsEWaYUkce24z4y2XFLjcUOFH6kWBjLw8Dlu0drjbCw7PxJ9L_9L2P5W2rbLOiSZRp6OE5sh3PcybXGKF7u_mti3i9Hfn5_ifSw5S9KbV2mnMQUOKwMcIb7T3e6f9Oi8HNAP6rJfH5yTX6NeylUjvawkkO0A16F7fvcY-XzZRzpJbMzp1PsMnSyvZXhUHX-BDVnyFxRmxwW_wt1s74bKoSFl8RV5ZRiyAJVPV5mpRJhvlDIkhm2RmHqRgKUlKVO5LjDyM_0f3DDf3h1jUYkZNbktWjndYaQwn2KDTXoKzzv7g16FrvRbcJMAS2eVBrpCskT4cqQVHuC1QQihaKuu3UoG4KUyFYYYlc0yVLO5OsNTKhZfyFqaNZZgvRkW2CkzxWGQpTwMVS5FzFSYyF5HEw9IjHzYd4PUN1uNKUkPPlCIIiiZQyCBTaQOKvnNg2yAx_UN0c00tadLXF70DLQcn_fZF81wfO7BeQ6Xt01jqx9hxYKVCbXogHLqphsSzkk_wnP6A9Lef7imuhkaHG8kO0TcHfIP8uy9Gd9sD_PL97VPdhI8Y4PrkqHe8BgvVSyxqfVuH-cnNbfYDudAk3rBB_gDqzQOT |
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=Molecular+and+biochemical+characterization+of+the+tetralin+degradation+pathway+in+Rhodococcus+sp.+strain+TFB&rft.jtitle=Microbial+biotechnology&rft.au=Tom%C3%A1s%E2%80%90Gallardo%2C+Laura&rft.au=Santero%2C+Eduardo&rft.au=Camafeita%2C+Emilio&rft.au=Calvo%2C+Enrique&rft.date=2009-03-01&rft.pub=Blackwell+Publishing+Ltd&rft.issn=1751-7915&rft.eissn=1751-7915&rft.volume=2&rft.issue=2&rft.spage=262&rft.epage=273&rft_id=info:doi/10.1111%2Fj.1751-7915.2009.00086.x&rft_id=info%3Apmid%2F21261920&rft.externalDBID=PMC3815846 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1751-7915&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1751-7915&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1751-7915&client=summon |