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Article

Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro.

Molecular microbiology - 1 Nov 1996

Laskowska E, Kuczyńska-Wiśnik D, Skórko-Glonek J, Taylor A

Abstract excerpt

Thermally aggregated, endogenous proteins of Escherichia coli form a distinct fraction, denoted S, which is separable by sucrose-density-gradient centrifugation. It was shown earlier that DnaK, DnaJ, IbpA and IbpB heat-shock proteins are associated with the S fraction. Comparison of the rise and...

Topics

ATP-Dependent Proteases
Adenosine Triphosphatases
Bacterial Proteins
Caseins
Centrifugation, Density Gradient
Electrophoresis, Polyacrylamide Gel
Endopeptidase Clp
Escherichia coli
Escherichia coli Proteins
Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Gene Expression Regulation, Enzymologic

Genetic Variation

HSP40 Heat-Shock Proteins

HSP70 Heat-Shock Proteins

Heat-Shock Proteins

Kinetics

Manganese

Periplasmic Proteins

Source

Identifiers

PMID: 8939438
DOI: 10.1046/j.1365-2958.1996.1231493.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8939438-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro.PMID 8939438Read ↗

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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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The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.Semantic proximity Read ↗

The proteolytic activity of the HtrA (DegP) protein from Escherichia coli at low temperatures.Semantic proximity Read ↗

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