Proteomics

Dataset Information

0

O The CutRS two-component system controls the Streptomyces secretion stress response by monitoring extracellular disulphide bond formation


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

Dataset's files

Source:
Action DRS
190516_05.raw Raw
190530_01_20190530222353.raw Raw
190530_02_20190531003921.raw Raw
190530_03_20190531025428.raw Raw
190530_04_20190531050952.raw Raw
Items per page:
1 - 5 of 44

Similar Datasets

2024-01-22 | PXD043651 | Pride
2024-01-22 | PXD044034 | Pride
2025-08-28 | PXD064199 | Pride
2025-08-28 | PXD048844 | Pride
2025-05-07 | PXD060769 | Pride
2025-08-05 | PXD061171 | Pride
2024-08-28 | PXD055051 | Pride
2023-06-16 | PXD040579 | Pride
2024-01-22 | PXD037917 | Pride
2024-01-22 | PXD043957 | Pride