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.

Abstract excerpt

The first discovery of an Hsp70 chaperone gene was the isolation of an Escherichia coli mutant, dnaK756, which rendered the cells resistant to lytic infection with bacteriophage lambda. The DnaK756 mutant protein has since been used to establish many of the cellular roles and biochemical properties of DnaK. DnaK756 has three glycine-to-aspartate substitutions at residues 32, 455, and 468, which were reported to...

Topics

• Adenosine Diphosphate
• Adenosine Triphosphatases
• Adenosine Triphosphate
• Escherichia coli Proteins
• HSP70 Heat-Shock Proteins
• Hydrolysis
• Luciferases
• Models, Molecular
• Molecular Chaperones
• Mutation
• Protein Binding
• Protein Conformation