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Article

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

The Journal of biological chemistry - 29 Oct 2010

Sohn Jungsan, Grant Robert A, Sauer Robert T

Abstract excerpt

DegS is a periplasmic Escherichia coli protease, which functions as a trimer to catalyze the initial rate-limiting step in a proteolytic cascade that ultimately activates transcription of stress response genes in the cytoplasm. Each DegS subunit consists of a protease domain and a PDZ domain. Dur...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20739286
DOI: 10.1074/jbc.M110.135541
PMCID: PMC2962503

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20739286-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.PMID 20739286Read ↗

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 ↗

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

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

Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine.Semantic proximity Read ↗

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

The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.Semantic proximity Read ↗

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

Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.Semantic proximity Read ↗

Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR.Semantic proximity Read ↗

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