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ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria

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ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria

Auteurs : Andrew N. Keller [Australie] ; Xiao Yang [Australie] ; Jana Wiedermannová [République tchèque] ; Olivier Delumeau [France] ; Libor Krásn [République tchèque] ; Peter J. Lewis [Australie]

Source :

Journal of Bacteriology [ 0021-9193 ] ; 2014.

RBID : PMC:4187704

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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4187704

DOI: 10.1128/JB.02020-14
PubMed: 25092033
PubMed Central: 4187704

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Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>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 <named-content content-type="genus-species">Firmicutes</named-content>
 phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω<sub>1</sub>
) 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.</p>
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  <front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id>
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School of Environmental and Life Sciences, University of Newcastle, Callghan, New South Wales, Australia</aff>
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Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic</aff>
<aff id="aff3"><label>c</label>
INRA, UMR-1319 Micalis, Jouy-en-Josas, France</aff>
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<author-notes><corresp id="cor1">Address correspondence to Peter J. Lewis, <email>Peter.Lewis@newcastle.edu.au</email>
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<pub-date pub-type="ppub"><month>10</month>
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<volume>196</volume>
<issue>20</issue>
<fpage>3622</fpage>
<lpage>3632</lpage>
<history><date date-type="received"><day>23</day>
<month>6</month>
<year>2014</year>
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<date date-type="accepted"><day>31</day>
<month>7</month>
<year>2014</year>
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<permissions><copyright-statement>Copyright © 2014, American Society for Microbiology. All Rights Reserved.</copyright-statement>
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<abstract><p>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 <named-content content-type="genus-species">Firmicutes</named-content>
 phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω<sub>1</sub>
) 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.</p>
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ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria

ε, a New Subunit of RNA Polymerase Found in Gram-Positive Bacteria

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