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Article

Allosteric regulation of DegS protease subunits through a shared energy landscape.

Nature chemical biology - 1 Feb 2013

Mauldin Randall V, Sauer Robert T

Abstract excerpt

The PDZ domains of the trimeric DegS protease bind unassembled outer-membrane proteins (OMPs) that accumulate in the Escherichia coli periplasm. This cooperative binding reaction triggers a proteolytic cascade that activates a transcriptional stress response. To dissect the mechanism of allosteric activation, we generated hybrid DegS trimers with different numbers of PDZ domains and/or protease-domain mutations....

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Share to Allosteric Site
Share to Catalytic Domain
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Gene Expression Regulation, Bacterial

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Source

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Identifiers

PMID: 23201899
DOI: 10.1038/nchembio.1135
PMCID: PMC3551985

Genes

OMP

Provenance

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allosteric regulation of DegS protease subunits through a shared energy landscape.PMID 23201899Read ↗

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

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

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 ↗

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

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

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

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

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