ArticleMicrobiology (Reading, England)2016
Characterization of a protein-protein interaction within the SigO-RsoA two-subunit σ factor: the σ70 region 2.3-like segment of RsoA mediates interaction with SigO.
Article in Microbiology (Reading, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Systematic modulation of bacterial resource allocation by perturbing RNA polymerase availability via synthetic transcriptional switches.Nucleic acids research · 2025Article
- Chimeric MerR-Family Regulators and Logic Elements for the Design of Metal Sensitive Genetic Circuits inACS synthetic biology · 2023Article
- Extracytoplasmic Function σ Factors as Tools for Coordinating Stress Responses.International journal of molecular sciences · 2021Review
- Expansion and re-classification of the extracytoplasmic function (ECF) σ factor family.Nucleic acids research · 2021Article
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9 authors at 1 institution in 1 country.
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Abstract
σ factors are single subunit general transcription factors that reversibly bind core RNA polymerase and mediate gene-specific transcription in bacteria. Previously, an atypical two-subunit σ factor was identified that activates transcription from a group of related promoters in Bacillus subtilis. Both of the subunits, named SigO and RsoA, share primary sequence similarity with the canonical σ70 family of σ factors and interact with each other and with RNA polymerase subunits. Here we show that the σ70 region 2.3-like segment of RsoA is unexpectedly sufficient for interaction with the amino-terminus of SigO and the β' subunit. A mutational analysis of RsoA identified aromatic residues conserved amongst all RsoA homologues, and often amongst canonical σ factors, that are particularly important for the SigO-RsoA interaction. In a canonical σ factor, region 2.3 amino acids bind non-template strand DNA, trapping the promoter in a single-stranded state required for initiation of transcription. Accordingly, we speculate that RsoA region 2.3 protein-binding activity likely arose from a motif that, at least in its ancestral protein, participated in DNA-binding interactions.
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