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Article

Physiological roles of the DnaK and GroE stress proteins: catalysts of protein folding or macromolecular sponges?

Molecular microbiology - 1 Mar 1991

LaRossa R A, Van Dyk T K

Abstract excerpt

When organisms ranging from microbes to man are subjected to certain environmental stresses a characteristic 'heat shock' response is observed. In Escherichia coli this response is characterized by the induction of several proteins, three of which are the 70 kilodalton product of the dnaK gene, the 60 kilodalton product of the groEL (mopA) gene and the 15 kilodalton product of the groES (mopB) gene. In this...

Topics

Bacterial Proteins
Chaperonins
Enterobacteriaceae
Escherichia coli Proteins
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Hot Temperature
Mutation
Protein Conformation

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2046546
DOI: 10.1111/j.1365-2958.1991.tb00724.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2046546-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Physiological roles of the DnaK and GroE stress proteins: catalysts of protein folding or macromolecular sponges?PMID 2046546Read ↗

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Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon.Semantic proximity Read ↗

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Comparative analysis of the molecular mechanism of heat shock proteins from pathogenic and non-pathogenic <i>E.coli</i>Semantic proximity Read ↗

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