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Article

Allosteric activation of DegS, a stress sensor PDZ protease.

Cell - 2 Nov 2007

Sohn Jungsan, Grant Robert A, Sauer Robert T

Abstract excerpt

Regulated intramembrane proteolysis is a method for transducing signals between cellular compartments. When protein folding is compromised in the periplasm of E. coli, the C termini of outer-membrane proteins (OMPs) bind to the PDZ domains of the trimeric DegS protease and activate cleavage of RseA, a transmembrane transcriptional regulator. We show here that DegS is an allosteric enzyme. OMP binding shifts the...

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Source

Identifiers

PMID: 17981123
DOI: 10.1016/j.cell.2007.08.044

Genes

OMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Allosteric activation of DegS, a stress sensor PDZ protease.PMID 17981123Read ↗

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

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

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

A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli.Semantic proximity Read ↗

Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress.Semantic proximity Read ↗

Dispensable PDZ domain of Escherichia coli YaeL essential protease.Semantic proximity Read ↗

DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response.Semantic proximity Read ↗

Unique residues involved in activation of the multitasking protease/chaperone HtrA from Chlamydia trachomatis.Semantic proximity Read ↗

PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease.Semantic proximity Read ↗

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