ArticleNucleic acids research2019
Alternative σI/anti-σI factors represent a unique form of bacterial σ/anti-σ complex.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 27 citations in OpenAlex.
- Learning Protein-Protein Binding Free Energies from Interface Graphs and Physicochemical Descriptors.ACS physical chemistry Au · 2026Article
- An uncharacterized small protein MicN mediates the transcriptional reprogramming of Salmonella through regulating the RpoS-RNA polymerase interaction.Communications biology · 2025Article
- The final proteolytic step in transmembrane signaling of multiple RsgI anti-σ factors in Clostridium thermocellum.Bioscience reports · 2025Article
- Unique Fn3-like biosensor in σProtein science : a publication of the Protein Society · 2024Article
- Composition of Lignocellulose Hydrolysate in Different Biorefinery Strategies: Nutrients and Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- A cellulosomal double-dockerin module from Clostridium thermocellum shows distinct structural and cohesin-binding features.Protein science : a publication of the Protein Society · 2024Article
- Structure of the transcription open complex of distinct σNature communications · 2023Article
- Essential autoproteolysis of bacterial anti-σ factor RsgI for transmembrane signal transduction.Science advances · 2023Article
- Article
- The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing.Proteins · 2022Article
- Unifying themes and distinct features of carbon and nitrogen assimilation by polysaccharide-degrading bacteria: a summary of four model systems.Applied microbiology and biotechnology · 2021Review
- c-di-GMP Arms an Anti-σ to Control Progression of Multicellular Differentiation in Streptomyces.Molecular cell · 2020Article
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Authors and funding
16 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The σ70 family alternative σI factors and their cognate anti-σI factors are widespread in Clostridia and Bacilli and play a role in heat stress response, virulence, and polysaccharide sensing. Multiple σI/anti-σI factors exist in some lignocellulolytic clostridial species, specifically for regulation of components of a multienzyme complex, termed the cellulosome. The σI and anti-σI factors are unique, because the C-terminal domain of σI (SigIC) and the N-terminal inhibitory domain of anti-σI (RsgIN) lack homology to known proteins. Here, we report structure and interaction studies of a pair of σI and anti-σI factors, SigI1 and RsgI1, from the cellulosome-producing bacterium, Clostridium thermocellum. In contrast to other known anti-σ factors that have N-terminal helical structures, RsgIN has a β-barrel structure. Unlike other anti-σ factors that bind both σ2 and σ4 domains of the σ factors, RsgIN binds SigIC specifically. Structural analysis showed that SigIC contains a positively charged surface region that recognizes the promoter -35 region, and the synergistic interactions among multiple interfacial residues result in the specificity displayed by different σI/anti-σI pairs. We suggest that the σI/anti-σI factors represent a distinctive mode of σ/anti-σ complex formation, which provides the structural basis for understanding the molecular mechanism of the intricate σI/anti-σI system.
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