Article
The 70-kDa heat-shock protein/DnaK chaperone system is required for the productive folding of ribulose-biphosphate carboxylase subunits in Escherichia coli.
European journal of biochemistry - 15 Sept 1997
Checa S K, Viale A M
Abstract excerpt
We have studied the in vivo requirements of the DnaK chaperone system for the folding of recombinant ribulose-bisphosphate carboxylase/oxygenase in Escherichia coli. Expression of functional dimeric or hexadecameric ribulose-bisphosphate carboxylase from different bacterial sources (including purple bacteria and cyanobacteria) was severely impaired in E. coli dnaK, dnaJ, or grpE mutants. These enzymes were...
Topics
- Bacterial Proteins
- Chaperonins
- Cyanobacteria
- Dimerization
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression Regulation, Bacterial
- HSP70 Heat-Shock Proteins
- Immunoblotting
- Molecular Chaperones
- Mutation
- Protein Conformation
- Protein Folding
- Recombinant Proteins
- Ribulose-Bisphosphate Carboxylase
- Temperature