Coevolutionary Analysis Reveals a Conserved Dual Binding Interface between Extracytoplasmic Function σ Factors and Class I Anti-σ Factors.
RNA polymerase
coevolutionary analysis
comparative genomics
computational biology
direct coupling analysis
gene regulation
transcription factors
Journal
mSystems
ISSN: 2379-5077
Titre abrégé: mSystems
Pays: United States
ID NLM: 101680636
Informations de publication
Date de publication:
04 Aug 2020
04 Aug 2020
Historique:
entrez:
6
8
2020
pubmed:
6
8
2020
medline:
6
8
2020
Statut:
epublish
Résumé
Extracytoplasmic function σ factors (ECFs) belong to the most abundant signal transduction mechanisms in bacteria. Among the diverse regulators of ECF activity, class I anti-σ factors are the most important signal transducers in response to internal and external stress conditions. Despite the conserved secondary structure of the class I anti-σ factor domain (ASDI) that binds and inhibits the ECF under noninducing conditions, the binding interface between ECFs and ASDIs is surprisingly variable between the published cocrystal structures. In this work, we provide a comprehensive computational analysis of the ASDI protein family and study the different contact themes between ECFs and ASDIs. To this end, we harness the coevolution of these diverse protein families and predict covarying amino acid residues as likely candidates of an interaction interface. As a result, we find two common binding interfaces linking the first alpha-helix of the ASDI to the DNA-binding region in the σ
Identifiants
pubmed: 32753504
pii: 5/4/e00310-20
doi: 10.1128/mSystems.00310-20
pmc: PMC7406223
pii:
doi:
Types de publication
Journal Article
Langues
eng
Informations de copyright
Copyright © 2020 Casas-Pastor et al.
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