AustralieFrV1, Ncbi, Checkpoint, bibRecord, 001C93

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

Identifieur interne : 001C93 ( Ncbi/Checkpoint ); précédent : 001C92; suivant : 001C94

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

Descripteurs français

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.

Url:

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

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

Affiliations:

Links to Exploration step

PMC:4187704

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>
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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

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

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