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.

doi:10.1073/pnas.89.15.7139

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

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.

Proceedings of the National Academy of Sciences of the United States of America - 1 Aug 1992

Wild J, Kamath-Loeb A, Ziegelhoffer E, Lonetto M, Kawasaki Y, Gross C A

Abstract excerpt

A set of 37 mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, was isolated using a selection for high constitutive expression of heat shock proteins. Of these, 11 mutants were able to carry out some but not all functions of DnaK. These partial function mutants w...

Topics

Amino Acid Sequence
Bacterial Proteins
Bacteriophage lambda
Chloramphenicol O-Acetyltransferase
DNA, Bacterial
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Genes, Dominant
Genes, Lethal
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Isopropyl Thiogalactoside

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phenotype

Temperature

Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 1386674
DOI: 10.1073/pnas.89.15.7139
PMCID: PMC49661

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1386674-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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