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 seri...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- DNA Primers
- Escherichia coli
- Escherichia coli Proteins
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Molecular Sequence Data
- Mutation
- Phenotype
- Sequence Analysis, DNA
- Temperature