ArticleNucleic acids research2013
Mycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of σ-factor activity by proteolysis.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Molecular basis of Streptomyces ECF σShbA factors transcribing principal σHrdB genes.Nucleic acids research · 2025Article
- Control of Toxin-Antitoxin Systems by Proteases inFrontiers in molecular biosciences · 2021Review
- Selectivity among Anti-σ Factors byJournal of bacteriology · 2019Article
- The fused SnoaL_2 domain in the Mycobacterium tuberculosis sigma factor σJ modulates promoter recognition.Nucleic acids research · 2017Article
- Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis.Current genetics · 2017Article
- Crystallographic studies of the extracytoplasmic function σ factor σ(J) from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Structural biology of bacterial RNA polymerase.Biomolecules · 2015Review
- Interactions between an anti-sigma protein and two sigma factors that regulate the pyoverdine signaling pathway in Pseudomonas aeruginosa.BMC microbiology · 2014Article
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4 authors at 1 institution in 1 country.
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Abstract
The relative levels of different σ factors dictate the expression profile of a bacterium. Extracytoplasmic function σ factors synchronize the transcriptional profile with environmental conditions. The cellular concentration of free extracytoplasmic function σ factors is regulated by the localization of this protein in a σ/anti-σ complex. Anti-σ factors are multi-domain proteins with a receptor to sense environmental stimuli and a conserved anti-σ domain (ASD) that binds a σ factor. Here we describe the structure of Mycobacterium tuberculosis anti-σ(D) (RsdA) in complex with the -35 promoter binding domain of σ(D) (σ(D)4). We note distinct conformational features that enable the release of σ(D) by the selective proteolysis of the ASD in RsdA. The structural and biochemical features of the σ(D)/RsdA complex provide a basis to reconcile diverse regulatory mechanisms that govern σ/anti-σ interactions despite high overall structural similarity. Multiple regulatory mechanisms embedded in an ASD scaffold thus provide an elegant route to rapidly re-engineer the expression profile of a bacterium in response to an environmental stimulus.
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