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Article

Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli.

The EMBO journal - 1 Jan 1992

Sherman MYu, Goldberg A L

Abstract excerpt

The ability of Escherichia coli rapidly to degrade abnormal proteins is inhibited by mutations affecting any of several heat shock proteins (hsps). We therefore tested whether a short-lived mutant protein might become associated with hsps as part of its degradation. At 30 degrees C, the non-secreted mutant form of alkaline phosphatase, phoA61, is relatively stable, and very little phoA61 is found associated with...

Topics

ATP-Dependent Proteases
Alkaline Phosphatase
Bacterial Proteins
Escherichia coli
Escherichia coli Proteins
HSP40 Heat-Shock Proteins
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Macromolecular Substances
Mutation
Protease La

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Serine Endopeptidases

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Identifiers

PMID: 1740117
DOI: 10.1002/j.1460-2075.1992.tb05029.x
PMCID: PMC556427

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1740117-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli.PMID 1740117Read ↗

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