Article
Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein.
The Journal of biological chemistry - 10 Nov 2006
Bird Jeremy G, Sharma Suveena, Roshwalb Sara C, Hoskins Joel R, Wickner Sue
Abstract excerpt
DnaK/Hsp70 proteins are universally conserved ATP-dependent molecular chaperones that help proteins adopt and maintain their native conformations. DnaJ/Hsp40 and GrpE are co-chaperones that assist DnaK. CbpA is an Escherichia coli DnaJ homolog. It acts as a multicopy suppressor for dnaJ mutations and functions in vitro in combination with DnaK and GrpE in protein remodeling reactions. CbpA binds nonspecifically...
Topics
- Bacterial Proteins
- Carrier Proteins
- Cross-Linking Reagents
- DNA Helicases
- DNA, Bacterial
- DNA-Binding Proteins
- Escherichia coli
- Escherichia coli Proteins
- HSP40 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Luciferases
- Molecular Chaperones
- Mutagenesis, Site-Directed