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A General Mechanism for Initiating the General Stress Response in Bacteria
Open accessPreprint — published as 10.7554/elife.100376.3 · Paper page
Abstract
The General Stress Response promotes survival of bacteria in adverse conditions, but how sensor proteins transduce species-specific signals to initiate the response is not known. The serine/threonine phosphatase RsbU initiates the General Stress Response in B. subtilis upon binding a partner protein (RsbT) that is released from sequestration by environmental stresses. We report that RsbT activates RsbU by inducing otherwise flexible linkers of RsbU to form a short coiled-coil that dimerizes and activates the phosphatase domains. Importantly, we present evidence that related coiled-coil linkers and phosphatase dimers transduce signals from diverse sensor domains to control the General Stress Response and other signaling across bacterial phyla. This coiled-coil linker transduction mechanism additionally suggests a resolution to the mystery of how shared sensory domains control serine/threonine phosphatases, diguanylate cyclases and histidine kinases. We propose that this provides bacteria with a modularly exchangeable toolkit for the evolution of diverse signaling pathways.
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Metadata
- Authors
- Baral, R., Ho, K., Kumar, R. P., Hopkins, J. B., Watkins, M. B., LaRussa, S., Caban-Penix, S., Calderone, L. A., & Bradshaw, N.
- Affiliations
- Brandeis University (US)
- Illinois Institute of Technology (US)
- Corresponding author
- Bradshaw, Niels
- ORCID
- Venue
- eLife
- Publisher
- openRxiv
- Published
- 2024-02-17
- Volume
- 13
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC12143880
- OpenAlex
- W4391917866
- Cited by
- 7
- References
- 2
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2
- Type
- posted content
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Energy (DE‐ AC02‐06CH11357, AC02‐06CH11357, 06CH11357, P30 GM138395, DE-AC02-)
- State University of New York
- Brandeis University
- National Institutes of Health (DE-AC02–06CH11357, 1s10od018090-01)
- Office of Science (AC02‐06CH11357, DE-AC02, 06CH11357, DE-AC02-06CH11357)
- University at Albany
- National Institute of General Medical Sciences (GM138395, T32GM007122, 1S10OD018090, DE-AC02-06CH11357, T32GM135126, P30GM138395, GM007122)
- Argonne National Laboratory (DE- AC02-06-CH11357, DE-AC02, AC02–06CH11357, 06CH11357, 1S10OD018090, P30 GM138395)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- general stress response, RsbU, serine/threonine phosphatase, protein dimerization, signal transduction, sensor proteins, Bacillus subtilis, diguanylate cyclase, histidine kinase
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