ε, a new subunit of RNA polymerase found in gram-positive bacteria.
Identifieur interne : 003394 ( PubMed/Corpus ); précédent : 003393; suivant : 003395ε, a new subunit of RNA polymerase found in gram-positive bacteria.
Auteurs : Andrew N. Keller ; Xiao Yang ; Jana Wiedermannová ; Olivier Delumeau ; Libor Krásn ; Peter J. LewisSource :
- Journal of bacteriology [ 1098-5530 ] ; 2014.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Bacillus subtilis (enzymology), DNA-Directed RNA Polymerases (chemistry), DNA-Directed RNA Polymerases (genetics), DNA-Directed RNA Polymerases (metabolism), Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Subunits.
- MESH :
- chemical , chemistry : DNA-Directed RNA Polymerases.
- enzymology : Bacillus subtilis.
- chemical , genetics : DNA-Directed RNA Polymerases.
- chemical , metabolism : DNA-Directed RNA Polymerases.
- Amino Acid Sequence, Animals, Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Subunits.
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.
DOI: 10.1128/JB.02020-14
PubMed: 25092033
Links to Exploration step
pubmed:25092033Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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