ArticleProteins2024
Insight into the autoproteolysis mechanism of the RsgI9 anti-σ factor from Clostridium thermocellum.
Article in Proteins, 2024. 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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Who cites it
4 citing papers in PubMed, 2 citations in OpenAlex.
- Microbial GAIN domains undergo autoproteolysis and enable release of diverse cell-surface-associated proteins.Current biology : CB · 2026Article
- Visual exoproteomics ofbioRxiv : the preprint server for biology · 2026Article
- 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
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Clostridium thermocellum is a potential microbial platform to convert abundant plant biomass to biofuels and other renewable chemicals. It efficiently degrades lignocellulosic biomass using a surface displayed cellulosome, a megadalton sized multienzyme containing complex. The enzymatic composition and architecture of the cellulosome is controlled by several transmembrane biomass-sensing RsgI-type anti-σ factors. Recent studies suggest that these factors transduce signals from the cell surface via a conserved RsgI extracellular (CRE) domain (also called a periplasmic domain) that undergoes autoproteolysis through an incompletely understood mechanism. Here we report the structure of the autoproteolyzed CRE domain from the C. thermocellum RsgI9 anti-σ factor, revealing that the cleaved fragments forming this domain associate to form a stable α/β/α sandwich fold. Based on AlphaFold2 modeling, molecular dynamics simulations, and tandem mass spectrometry, we propose that a conserved Asn-Pro bond in RsgI9 autoproteolyzes via a succinimide intermediate whose formation is promoted by a conserved hydrogen bond network holding the scissile peptide bond in a strained conformation. As other RsgI anti-σ factors share sequence homology to RsgI9, they likely autoproteolyze through a similar mechanism.
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Registered trials
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