ε, a new subunit of RNA polymerase found in gram-positive bacteria
| Autor: | Libor Krasny, Xiao Yang, Peter J. Lewis, Jana Wiedermannová, Andrew N. Keller, Olivier Delumeau |
|---|---|
| Přispěvatelé: | School of Environmental and Life Sciences, Newcastle University [Newcastle], Czech Academy of Sciences [Prague] (ASCR), MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Czech Academy of Sciences [Prague] (CAS) |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Protein Conformation [SDV]Life Sciences [q-bio] Molecular Sequence Data RNA-dependent RNA polymerase RNA polymerase II Microbiology Gene Expression Regulation Enzymologic chemistry.chemical_compound Transcription (biology) RNA polymerase RNA polymerase I Animals Amino Acid Sequence Molecular Biology Phylogeny Polymerase biology DNA-Directed RNA Polymerases Gene Expression Regulation Bacterial Articles Molecular biology 3. Good health Protein Subunits chemistry biology.protein Transcription factor II D Small nuclear RNA Bacillus subtilis |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2014, 196 (20), pp.3622-3632. ⟨10.1128/JB.02020-14⟩ |
| ISSN: | 0021-9193 1098-5530 |
| DOI: | 10.1128/JB.02020-14⟩ |
| Popis: | 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 epsilon. Previously epsilon had been identified as a small protein (omega(1)) that copurified with RNA polymerase. We have solved the structure of epsilon by X-ray crystallography and show that it is not an omega subunit. Rather, epsilon bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of epsilon shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of epsilon 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 epsilon with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that epsilon may serve a role in protection from phage infection. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|