Article
Genetic and biochemical characterization of mutations affecting the carboxy-terminal domain of the Escherichia coli molecular chaperone DnaJ.
Molecular microbiology - 1 Oct 1998
Goffin L, Georgopoulos C
Abstract excerpt
DnaJ is a universally conserved heat shock protein involved in protein folding. DnaJ contains four conserved domains. The N-terminal 'J-domain' has been shown to be responsible for the recruitment of its specific DnaK partner protein. The 'Gly/Phe'- and 'Cys-rich' domains have been implicated in...
Topics
- Amino Acid Sequence
- Bacteriophage lambda
- Cell Division
- Conserved Sequence
- Down-Regulation
- Escherichia coli
- Escherichia coli Proteins
- HSP40 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Heat-Shock Response
- Luciferases
- Molecular Sequence Data
- Mutation
- Sequence Deletion
- Sigma Factor
- Transcription Factors