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Article

Isolation and characterization of an Escherichia coli DnaK mutant with impaired ATPase activity.

Journal of molecular biology - 30 Sept 1994

Burkholder W F, Panagiotidis C A, Silverstein S J, Cegielska A, Gottesman M E, Gaitanaris G A

Abstract excerpt

A temperature-sensitive mutant of DnaK, the principal Escherichia coli member of the 70 kDa heat shock protein family, has been isolated. The mutation, dnaK25, lies in the putative ATP binding pocket of DnaK. It consists of a C to T transition that changes the highly conserved proline 143 to serine. Mutant strains do not support the propagation of bacteriophage lambda or of plasmids that require DnaA for...

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PMID: 7932696
DOI: 10.1006/jmbi.1994.1587

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Isolation and characterization of an Escherichia coli DnaK mutant with impaired ATPase activity.PMID 7932696Read ↗

Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis.Semantic proximity Read ↗

Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling.Semantic proximity Read ↗

Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.Semantic proximity Read ↗

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The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein.Semantic proximity Read ↗

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