PXD051851 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | o The CutRS two-component system controls the Streptomyces secretion stress response by monitoring extracellular disulphide bond formation |
| Description | 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. |
| HostingRepository | PRIDE |
| AnnounceDate | 2025-08-09 |
| AnnouncementXML | Submission_2025-08-09_09:42:01.590.xml |
| DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD051851 |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Supported dataset by repository |
| PrimarySubmitter | Gerhard Saalbach |
| SpeciesList | scientific name: Streptomyces venezuelae; NCBI TaxID: 54571; |
| ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
| Instrument | Orbitrap Fusion |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2024-04-29 10:37:29 | ID requested | |
| ⏵ 1 | 2025-08-09 09:42:01 | announced | |
Publication List
Keyword List
| submitter keyword: proteomics, Two component systems, cutRS,Streptomyces, Secretion stress, Regulation |
Contact List
| Matt Hutchings |
| contact affiliation | Department Molecular Microbiology John Innes Centre Norwich Research Park Norwich, UK |
| contact email | matt.hutchings@jic.ac.uk |
| lab head | |
| Gerhard Saalbach |
| contact affiliation | Biological Chemistry |
| contact email | gerhard.saalbach@jic.ac.uk |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/08/PXD051851 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD051851
- Label: PRIDE project
- Name: o The CutRS two-component system controls the Streptomyces secretion stress response by monitoring extracellular disulphide bond formation