Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P51532 (transcriptional activator)
 6,546 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The expression of heat shock genes in Escherichia coli is regulated by the antagonistic action of the transcriptional activator, the sigma32 subunit of RNA polymerase, and negative modulators. Modulators are the DnaK chaperone system, which inactivates and destabilizes sigma32, and the FtsH protease, which is largely responsible for sigma32 degradation. A yet unproven hypothesis is that the degree of sequestration of the modulators through binding to misfolded proteins determines the level of heat shock gene transcription. This hypothesis was tested by altering the modulator concentration in cells expressing dnaK, dnaJ and ftsH from IPTG and arabinose-controlled promoters. Small increases in levels of DnaK and the DnaJ co-chaperone (< 1.5-fold of wild type) resulted in decreased level and activity of sigma32 at intermediate temperature and faster shut-off of the heat shock response. Small decreases in their levels caused inverse effects and, furthermore, reduced the refolding efficiency of heat-denatured protein and growth at heat shock temperatures. Fewer than 1500 molecules of a substrate of the DnaK system, structurally unstable firefly luciferase, resulted in elevated levels of heat shock proteins and a prolonged shut-off phase of the heat shock response. In contrast, a decrease in FtsH levels increased the sigma32 levels, but the accumulated sigma32 was inactive, indicating that sequestration of FtsH alone cannot induce the heat shock response efficiently. DnaK and DnaJ thus constitute the primary stress-sensing and transducing system of the E. coli heat shock response, which detects protein misfolding with high sensitivity.
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PMID:Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. 982 22

For lysogenization of Escherichia coli cells by bacteriophage lambda, functions of three lambda genes called c are necessary. The cI gene codes for a repressor that blocks activities of lytic promoters. However, early after infection, expression of cI is dependent on the function of the cII gene, coding for a specific transcriptional activator. The cII protein is unstable in E. coli cells due to FtsH-mediated proteolysis. The cIII gene product is an inhibitor of the FtsH protease. Here we demonstrate that cIII may have another function apart from inhibition of cII degradation. We found that overexpression of the cII gene results in impaired lysogenization by phage lambda, however simultaneous overexpression of the cIII gene abolished this negative effect on lysogenization. Analysis of cII-mediated transcriptional activation of certain promoters at different levels of cII and cIII proteins in cells confirmed that observed effects cannot be explained assuming that the only role of cIII is inhibition of FtsH-mediated degradation of cII. We propose that cIII has an additional role apart from its well-known function in indirect stabilization of cII. Apparently, cIII influences not only cII level but also activity of this transcriptional stimulator, especially at its high concentrations.
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PMID:Bacteriophage lambda cIII gene product has an additional function apart from inhibition of cII degradation. 1132 48