O The CutRS two-component system controls the Streptomyces secretion stress response by monitoring extracellular disulphide bond formation
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ABSTRACT: o Translocating unfolded proteins across cell membranes is essential in all domains of life and requires the conserved Sec machinery. In bacteria, Sec substrates fold on the extracellular face of the cytoplasmic membrane and misfolding triggers a stress response that involves production of HtrA-family proteins that act as dual function chaperone-proteases. In monoderm bacteria such as Streptomyces species, Sec substrates are translocated directly into the oxidising environment and typically contain even numbers of cysteine residues that form disulphide bonds to help the proteins fold. The Streptomyces secretion stress response is mediated by conserved two-component systems CssRS and CutRS and here we provide evidence that CutS senses disulphide bond formation via two conserved cysteine residues in its extracellular sensor domain. Breaking this disulphide bond activates CutRS and modulates the production of the quality control chaperones HtrA3 and HtrB. To our knowledge this represents a unique extracellular a sensing mechanism in bacteria.
INSTRUMENT(S):
ORGANISM(S): Streptomyces Venezuelae
TISSUE(S): Cell Culture
SUBMITTER:
Gerhard Saalbach
LAB HEAD: Matt Hutchings
PROVIDER: PXD051851 | Pride | 2025-08-09
REPOSITORIES: Pride
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