ArticleScientific reports2016
A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ32.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Spatial Chromosome Organization and Adaptation ofMicroorganisms · 2024Article
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- Toward the Complete Functional Characterization of a Minimal Bacterial Proteome.The journal of physical chemistry. B · 2022Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Article
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- Lon Protease Removes Excess Signal Recognition Particle Protein in Escherichia coli.Journal of bacteriology · 2020Article
- Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.eLife · 2020Article
- A photo-cross-linking approach to monitor folding and assembly of newly synthesized proteins in a living cell.The Journal of biological chemistry · 2018Article
- A novel plant E3 ligase stabilizes Escherichia coli heat shock factor σScientific reports · 2017Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- Regulation of bacterial heat shock stimulons.Cell stress & chaperones · 2016Review
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Authors and funding
6 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Heat shock response (HSR) generally plays a major role in sustaining protein homeostasis. In Escherichia coli, the activity and amount of the dedicated transcription factor σ(32) transiently increase upon heat shock. The initial induction is followed by chaperone-mediated negative feedback to inactivate and degrade σ(32). Previous work reported that signal recognition particle (SRP)-dependent targeting of σ(32) to the membrane is essential for feedback control, though how SRP recognizes σ(32) remained unknown. Extensive photo- and disulfide cross-linking studies in vivo now reveal that the highly conserved regulatory region of σ(32) that lacks a consecutive hydrophobic stretch interacts with the signal peptide-binding site of Ffh (the protein subunit of SRP). Importantly, the σ(32)-Ffh interaction observed was significantly affected by mutations in this region that compromise the feedback regulation, but not by deleting the DnaK/DnaJ chaperones. Homeostatic regulation of HSR thus requires a novel type of SRP recognition mechanism.
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