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PMID:1429436
| Citation |
Adar, YY, Simaan, M and Ulitzur, S (1992) Formation of the LuxR protein in the Vibrio fischeri lux system is controlled by HtpR through the GroESL proteins. J. Bacteriol. 174:7138-43 |
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| Abstract |
The transcription of the luminescence (lux) system of Vibrio fischeri is regulated by the LuxR protein and an autoinducer. We previously showed that apart from these regulatory elements, the transcription of the lux system is negatively controlled by the LexA protein and positively controlled by the HtpR protein (sigma 32). This study was conducted in order to elucidate the mode of action of the HtpR protein. Using luxR-lacZ fused genes, we showed that the HtpR protein is essential for the maximum expression of beta-galactosidase activity in Escherichia coli lac mutant cells. Using this construct, we also demonstrated that luxR is preferentially expressed toward the end of the logarithmic phase of growth. Starvation and addition of ethanol significantly advanced the appearance of beta-galactosidase activity in htpR+ cells. The luminescence system of E. coli htpR+ cells harboring the pChv1 plasmid with a deletion in the luxI gene is induced in the presence of low and constant concentrations (150 pg/ml) of the inducer only at a late stage of the logarithmic phase of growth. When the cellular LuxR content is reduced, following 23 generations of exponential growth in Luria broth, a mid-log-phase culture does not respond to the inducer (150 pg/ml). On the basis of the above observations we suggest that the HtpR protein controls the formation of V. fischeri LuxR protein. Preliminary findings indicate that the HtpR protein acts through the chaperonins GroESL. E. coli htpR/pChv1 cells retained their full level of in vivo and in vitro luciferase activities in the presence of multiple copies of groESL genes. The possibility that GroESL proteins stabilize the native form of LuxR protein is discussed. |
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| Keywords |
Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Chaperonins/genetics; Chaperonins/metabolism; Cloning, Molecular; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Gene Deletion; Genes, Bacterial; Heat-Shock Proteins; Luciferases/metabolism; Luminescent Measurements; Plasmids; Regulatory Sequences, Nucleic Acid; Repressor Proteins; Restriction Mapping; Serine Endopeptidases; Sigma Factor/genetics; Sigma Factor/metabolism; Trans-Activators; Transcription Factors; Transcription, Genetic; Vibrio/genetics; Vibrio/growth & development; Vibrio/metabolism; beta-Galactosidase/genetics; beta-Galactosidase/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0033554: cellular response to stress |
ECO:0000314: |
P |
figure 6 shows wild-type cells in stationary phase respond immediately to presence of inducer, whereas wild-type cells of other logarithmic growth phases do not. |
complete | ||||
| GO:0033554: cellular response to stress |
ECO:0000315: |
P |
figure 8: transforming groESL-containing plasmids into htpR mutant cells showed luminescence induction at a much earlier growth stage than wild-type cells without the plasmid. Luciferase activity of htpR mutant cells was fully recovered by presence of GroESL proteins. |
complete | ||||
See also
References
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