AustralieFrV1, PubMed, Curation, bibRecord, 003282

ε, a new subunit of RNA polymerase found in gram-positive bacteria.

Identifieur interne : 003282 ( PubMed/Curation ); précédent : 003281; suivant : 003283

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 [ 1098-5530 ] ; 2014.

RBID : pubmed:25092033

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.

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

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Le document en format XML

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<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
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<term>Régulation de l'expression des gènes bactériens</term>
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<term>Séquence d'acides aminés</term>
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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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<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName>
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	Serveur d'exploration sur les relations entre la France et l'Australie
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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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