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Article

Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress.

Genes & development - 15 Apr 2014

Kim Seokhee, Sauer Robert T

Abstract excerpt

Intracellular proteases combat proteotoxic stress by degrading damaged proteins, but their activity must be carefully controlled to maintain cellular fitness. The activity of Escherichia coli DegP, a highly conserved periplasmic protease, is regulated by substrate-dependent allosteric transformations between inactive and active trimer conformations and by the formation of polyhedral cages that confine the active...

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Share to Enzyme Activation
Share to Heat-Shock Proteins
Share to Hot Temperature

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microbial Viability

Share to Periplasmic Proteins

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Share to Serine Endopeptidases

Share to Stress, Physiological

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Identifiers

PMID: 24736846
DOI: 10.1101/gad.238394.114
PMCID: PMC4003281

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Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress.PMID 24736846Read ↗

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Altered expression of a quality control protease in E. coli reshapes the in vivo mutational landscape of a model enzyme.Semantic proximity Read ↗

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

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

Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations.Semantic proximity Read ↗

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

Proteolytically Coordinated Activation of Toxin-Antitoxin ModulesSemantic proximity Read ↗

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

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

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