4.8 Article

The tyrosine kinase McsB is a regulated adaptor protein for ClpCP

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EMBO JOURNAL
卷 26, 期 8, 页码 2061-2070

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NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7601655

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AAA plus proteins; adaptor proteins; heat shock regulation; proteolysis; tyrosine kinase

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Cells of the soil bacterium Bacillus subtilis have to adapt to fast environmental changes in their natural habitat. Here, we characterized a novel system in which cells respond to heat shock by regulatory proteolysis of a transcriptional repressor CtsR. In B. subtilis, CtsR controls the synthesis of itself, the tyrosine kinase McsB, its activator McsA and the Hsp100/Clp proteins ClpC, ClpE and their cognate peptidase ClpP. The AAA+ protein family members ClpC and ClpE can form an ATP-dependent protease complex with ClpP and are part of the B. subtilis protein quality control system. The regulatory response is mediated by a proteolytic switch, which is formed by these proteins under heat-shock conditions, where the tyrosine kinase McsB acts as a regulated adaptor protein, which in its phosphorylated form activates the Hsp100/Clp protein ClpC and targets the repressor CtsR for degradation by the general protease ClpCP.

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