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Article

Steric clashes with bound OMP peptides activate the DegS stress-response protease.

Proceedings of the National Academy of Sciences of the United States of America - 17 Mar 2015

de Regt Anna K, Baker Tania A, Sauer Robert T

Abstract excerpt

Escherichia coli senses envelope stress using a signaling cascade initiated when DegS cleaves a transmembrane inhibitor of a transcriptional activator for response genes. Each subunit of the DegS trimer contains a protease domain and a PDZ domain. During stress, unassembled outer-membrane proteins (OMPs) accumulate in the periplasm and their C-terminal peptides activate DegS by binding to its PDZ domains. In the...

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Identifiers

PMID: 25733864
DOI: 10.1073/pnas.1502372112
PMCID: PMC4371955

Genes

OMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Steric clashes with bound OMP peptides activate the DegS stress-response protease.PMID 25733864Read ↗

OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations.Semantic proximity Read ↗

Allosteric activation of DegS, a stress sensor PDZ protease.Semantic proximity Read ↗

Allosteric regulation of DegS protease subunits through a shared energy landscape.Semantic proximity Read ↗

Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.Semantic proximity Read ↗

Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP.Semantic proximity Read ↗

PDZ domains of RseP are not essential for sequential cleavage of RseA or stress-induced σ(E) activation in vivo.Semantic proximity Read ↗

Fine-Tuning of σE Activation Suppresses Multiple Assembly-Defective Mutations in Escherichia coli.Semantic proximity Read ↗

A structure-based model of substrate discrimination by a noncanonical PDZ tandem in the intramembrane-cleaving protease RseP.Semantic proximity Read ↗

Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival.Semantic proximity Read ↗

Structure of the periplasmic stress response protein CpxP.Semantic proximity Read ↗

Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture.Semantic proximity Read ↗

Structural basis of adaptor-mediated protein degradation by the tail-specific PDZ-protease Prc.Semantic proximity Read ↗

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