We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
GroEL/GroES chaperone and Lon protease regulate expression of the Vibrio fischeri lux operon in Escherichia coli.
- Authors
Manukhov, I. V.; Kotova, V. Yu.; Zavilgelsky, G. B.
- Abstract
Chaperone GroEL/GroES and Lon protease were shown to play a role in regulating the expression of the Vibrio fischeri lux operon cloned in Escherichia coli cells. The E. coli groE mutant carrying a plasmid with the full-length V. fischeri lux regulon showed a decreased bioluminescence. The bioluminescence intensity was high in E. coli cells with mutant lonA and the same plasmid. Bioluminescence induction curves lacked the lag period characteristic of lon + strains. Regulatory luxR of V. fischeri was cloned in pGEX-KG to produce the hybrid gene GST-luxR. The product of its expression, GST-LuxR, was isolated together with GroEL and Lon upon affinity chromatography on a column with glutathione-agarose, suggesting complexation of LuxR with these proteins. It was assumed that GroEL/GroES is involved in LuxR folding, while Lon protease degrades LuxR before its folding into an active globule or after denaturation.
- Subjects
MOLECULAR chaperones; PROTEOLYTIC enzymes; VIBRIO fischeri; ESCHERICHIA coli; OPERONS; BIOLUMINESCENCE
- Publication
Molecular Biology, 2006, Vol 40, Issue 2, p240
- ISSN
0026-8933
- Publication type
Article
- DOI
10.1134/S0026893306020099