首页> 美国卫生研究院文献>other >Two functions of the C-terminal domain of Escherichia coli Rob: mediating sequestration-dispersal as a novel off-on switch for regulating Rob’s activity as a transcription activator and preventing degradation of Rob by Lon protease
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Two functions of the C-terminal domain of Escherichia coli Rob: mediating sequestration-dispersal as a novel off-on switch for regulating Rob’s activity as a transcription activator and preventing degradation of Rob by Lon protease

机译:大肠杆菌Coli Rob的C末端域的两种功能:将螯合分散作为一种新型脱机开关用于调节ROB的活性作为转录激活物并通过LON蛋白酶预防RB的降解

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摘要

In Escherichia coli, Rob activates transcription of the SoxRS/MarA/Rob regulon. Previous work revealed that Rob resides in 3–4 immunostainable foci, that dipyridyl and bile salts are inducers of its activity, and that inducers bind to Rob’s C-terminal domain (CTD). We propose that sequestration inactivates Rob by blocking its access to the transcriptional machinery and that inducers activate Rob by mediating its dispersal, allowing interaction with RNA polymerase. To test “sequestration-dispersal” as a new mechanism for regulating the activity of transcriptional activators, we fused Rob’s CTD to SoxS and used indirect immunofluorescence microscopy to determine the effect of inducers on SoxS-Rob’s cellular localization. Unlike native SoxS, which is uniformly distributed throughout the cell, SoxS-Rob is sequestered without inducer, but is rapidly dispersed when cells are treated with inducer. In this manner, Rob’s CTD serves as an anti-sigma factor in regulating the co-sigma factor-like activity of SoxS when fused to it. Rob’s CTD also protects its N-terminus from Lon protease, since Lon’s normally rapid degradation of SoxS is blocked in the chimera. Accordingly, Rob’s CTD has novel regulatory properties that can be bestowed on another E. coli protein.

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