PMID:12446654
| Citation |
Lopes Ferreira, N and Alix, JH (2002) The DnaK chaperone is necessary for alpha-complementation of beta-galactosidase in Escherichia coli. J. Bacteriol. 184:7047-54 |
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| Abstract |
We show here the involvement of the molecular chaperone DnaK from Escherichia coli in the in vivo alpha-complementation of the beta-galactosidase. In the dnaK756(Ts) mutant, alpha-complementation occurs when the organisms are grown at 30 degrees C but not at 37 or 40 degrees C, although these temperatures are permissive for bacterial growth. Plasmid-driven expression of wild-type dnaK restores the alpha-complementation in the mutant but also stimulates it in a dnaK(+) strain. In a mutant which contains a disrupted dnaK gene (DeltadnaK52::Cm(r)), alpha-complementation is also impaired, even at 30 degrees C. This observation provides an easy and original phenotype to detect subtle functional changes in a protein such as the DnaK756 chaperone, within the physiologically relevant temperature. |
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| Keywords |
Amino Acid Sequence; Escherichia coli/enzymology; Escherichia coli Proteins/physiology; Genetic Complementation Test; HSP70 Heat-Shock Proteins/physiology; Immunoblotting; Molecular Sequence Data; beta-Galactosidase/genetics |
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