PMID:8817918
| Citation |
Peruski, LF Jr (1996) Expression of heat shock protein D 48.5 of Escherichia coli is subject to modulation by catabolite repression. Microbiol. Res. 151:273-80 |
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| Abstract |
The Escherichia coli heat shock regulon consists of approximately twenty polypeptides that are coordinately and transiently induced upon a temperature upshift under the control of an alternative sigma factor, designated sigma-32 or HtpR. Preliminary observations on one of the proteins of the heat shock response, protein D 48.5, suggested that its induction by sigma-32 during heat shock may be modulated by catabolite repression. In this study, a disk diffusion assay was used to screen the effect of several compounds on the expression of a lacZ fusion in the gene encoding protein D 48.5. This assay indicated that the expression of this protein was controlled, at least in part, by the catabolite repression response. A more indepth analysis of the expression of protein D 48.5 under both steady-state and heat shock conditions was conducted in both a wild type and cya crp background. This analysis revealed that in the cya crp background, the steady-state level of protein D 48.5 was elevated relative to the wildtype, but that the heat shock induction of the protein was reduced in magnitude relative to the wild type strain, suggesting a direct link between these two global responses. The lacZ fusion in the structural gene for protein D 48.5 should prove useful as a reporter mechanism to probe the physiology and regulation of the heat shock response. |
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| Keywords |
Cloning, Molecular; Electrophoresis, Gel, Two-Dimensional; Escherichia coli/genetics; Galactosidases/metabolism; Gene Expression Regulation, Bacterial/drug effects; Gene Expression Regulation, Bacterial/genetics; Heat-Shock Proteins/biosynthesis; Heat-Shock Proteins/genetics; Image Processing, Computer-Assisted; Lac Operon; Repressor Proteins/genetics |
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