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| Title | ε, a new subunit of RNA polymerase found in gram-positive bacteria. |
|---|---|
| Journal, issue, pages | J Bacteriol, Vol. 196, Issue 20, Page 3622-3632, Year 2014 |
| Publish date | Aug 4, 2014 |
 Authors | Andrew N Keller / Xiao Yang / Jana Wiedermannová / Olivier Delumeau / Libor Krásný / Peter J Lewis /    |
| PubMed 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 ...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. |
 External links | J Bacteriol / PubMed:25092033 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 2.3 - 24.0 Å |
| Structure data |  EMDB-2637:  PDB-4njc: |
| Chemicals |  ChemComp-HOH: |
| Source |
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 Keywords | TRANSCRIPTION / DNA Dependant RNA Polymerase |
Bacillus subtilis (bacteria)
geobacillus stearothermophilus (bacteria)