ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria
RNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) tha...
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Veröffentlicht in: | Journal of bacteriology 2014-10, Vol.196 (20), p.3622-3632 |
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creator | Keller, Andrew N Yang, Xiao Wiedermannová, Jana Delumeau, Olivier Krásný, Libor Lewis, Peter J |
description | RNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection. |
doi_str_mv | 10.1128/JB.02020-14 |
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We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection.</description><identifier>ISSN: 0021-9193</identifier><identifier>EISSN: 1098-5530</identifier><identifier>DOI: 10.1128/JB.02020-14</identifier><identifier>PMID: 25092033</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; Animals ; Bacillus subtilis - enzymology ; bacteriology ; bacteriophages ; DNA ; DNA-directed RNA polymerase ; DNA-Directed RNA Polymerases - chemistry ; DNA-Directed RNA Polymerases - genetics ; DNA-Directed RNA Polymerases - metabolism ; Firmicutes ; gene expression ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Gram-positive bacteria ; Life Sciences ; Models, Molecular ; Molecular Sequence Data ; phenotype ; Phylogeny ; Protein Conformation ; Protein Subunits ; proteins ; transcription (genetics) ; X-ray diffraction</subject><ispartof>Journal of bacteriology, 2014-10, Vol.196 (20), p.3622-3632</ispartof><rights>Copyright © 2014, American Society for Microbiology. All Rights Reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2014, American Society for Microbiology. All Rights Reserved. 2014 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-0046-832X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4187704/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4187704/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25092033$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01204433$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Keller, Andrew N</creatorcontrib><creatorcontrib>Yang, Xiao</creatorcontrib><creatorcontrib>Wiedermannová, Jana</creatorcontrib><creatorcontrib>Delumeau, Olivier</creatorcontrib><creatorcontrib>Krásný, Libor</creatorcontrib><creatorcontrib>Lewis, Peter J</creatorcontrib><title>ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria</title><title>Journal of bacteriology</title><addtitle>J Bacteriol</addtitle><description>RNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacillus subtilis - enzymology</subject><subject>bacteriology</subject><subject>bacteriophages</subject><subject>DNA</subject><subject>DNA-directed RNA polymerase</subject><subject>DNA-Directed RNA Polymerases - chemistry</subject><subject>DNA-Directed RNA Polymerases - genetics</subject><subject>DNA-Directed RNA Polymerases - metabolism</subject><subject>Firmicutes</subject><subject>gene expression</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Gram-positive bacteria</subject><subject>Life Sciences</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>phenotype</subject><subject>Phylogeny</subject><subject>Protein Conformation</subject><subject>Protein Subunits</subject><subject>proteins</subject><subject>transcription (genetics)</subject><subject>X-ray diffraction</subject><issn>0021-9193</issn><issn>1098-5530</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1O3EAMx0eICra0p97bOYJEqD3fuVRaVgWKVhQVOI8myQQGJRmaSbbiwfoaPFODllaFS2sfLNk__23LhLxDOEBk5uPp4QGwyTMUG2SGkJtMSg6bZAbAMMsx59vkdUq3ACiEZFtkm0nIGXA-I4uHn_vU0TP_g16MxdiFgcaafjub0_PY3Le-d8nTozh2FQ0dPe5dm53HFIaw8vTQlYPvg3tDXtWuSf7tU9whV0efLxcn2fLr8ZfFfJnVPIch8xzRyZqLvCoLLxWTzkOJ3vBCuwK1qfRkqKEUSglheFWpshKsLrUUTju-Qz6tde_GovVV6buhd42960Pr-nsbXbDPK124sddxZQUarUFMAntrgZsXbSfzpX3MATIQgvMVTuzu07A-fh99GmwbUumbxnU-jsmi0kZqVLn5D5QxBSCZ-DcqFQdpFFMT-v7va__s-_t3E_BhDdQuWnfdh2SvLhigfPyzBi74L0VUoQA</recordid><startdate>20141001</startdate><enddate>20141001</enddate><creator>Keller, Andrew N</creator><creator>Yang, Xiao</creator><creator>Wiedermannová, Jana</creator><creator>Delumeau, Olivier</creator><creator>Krásný, Libor</creator><creator>Lewis, Peter J</creator><general>American Society for Microbiology</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>7QL</scope><scope>7TM</scope><scope>C1K</scope><scope>7S9</scope><scope>L.6</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0046-832X</orcidid></search><sort><creationdate>20141001</creationdate><title>ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria</title><author>Keller, Andrew N ; Yang, Xiao ; Wiedermannová, Jana ; Delumeau, Olivier ; Krásný, Libor ; Lewis, Peter J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f390t-e311a5f349dcbe5625ae0c1e83b7ab178d7777170c4664483dd6cd42fc754a7a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacillus subtilis - enzymology</topic><topic>bacteriology</topic><topic>bacteriophages</topic><topic>DNA</topic><topic>DNA-directed RNA polymerase</topic><topic>DNA-Directed RNA Polymerases - chemistry</topic><topic>DNA-Directed RNA Polymerases - genetics</topic><topic>DNA-Directed RNA Polymerases - metabolism</topic><topic>Firmicutes</topic><topic>gene expression</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Gram-positive bacteria</topic><topic>Life Sciences</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>phenotype</topic><topic>Phylogeny</topic><topic>Protein Conformation</topic><topic>Protein Subunits</topic><topic>proteins</topic><topic>transcription (genetics)</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Keller, Andrew N</creatorcontrib><creatorcontrib>Yang, Xiao</creatorcontrib><creatorcontrib>Wiedermannová, Jana</creatorcontrib><creatorcontrib>Delumeau, Olivier</creatorcontrib><creatorcontrib>Krásný, Libor</creatorcontrib><creatorcontrib>Lewis, Peter J</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of bacteriology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Keller, Andrew N</au><au>Yang, Xiao</au><au>Wiedermannová, Jana</au><au>Delumeau, Olivier</au><au>Krásný, Libor</au><au>Lewis, Peter J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria</atitle><jtitle>Journal of bacteriology</jtitle><addtitle>J Bacteriol</addtitle><date>2014-10-01</date><risdate>2014</risdate><volume>196</volume><issue>20</issue><spage>3622</spage><epage>3632</epage><pages>3622-3632</pages><issn>0021-9193</issn><eissn>1098-5530</eissn><abstract>RNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high-A+T Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω1) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>25092033</pmid><doi>10.1128/JB.02020-14</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-0046-832X</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Bacillus subtilis - enzymology bacteriology bacteriophages DNA DNA-directed RNA polymerase DNA-Directed RNA Polymerases - chemistry DNA-Directed RNA Polymerases - genetics DNA-Directed RNA Polymerases - metabolism Firmicutes gene expression Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic Gram-positive bacteria Life Sciences Models, Molecular Molecular Sequence Data phenotype Phylogeny Protein Conformation Protein Subunits proteins transcription (genetics) X-ray diffraction |
title | ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria |
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