Dutta Sujit, Lewis Richard J
Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England.
Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):191-3. doi: 10.1107/s0907444902020723. Epub 2002 Dec 19.
The general stress response of Bacillus subtilis provides a protective resistance to a variety of pressures. The key molecule is a subunit of RNA polymerase, sigma(B), which confers promoter specificity and is regulated by two signalling modules. Each module comprises protein kinases and phosphatases and 'switch' protein substrates for the kinase and phosphatase. The phosphorylation state of the switch molecules indirectly controls the activity of sigma(B). The binding of the kinase RsbT to the phosphatase RsbU stimulates its enzymatic activity towards its substrate, phosphorylated RsbV. To understand how these enzymes interact, thus regulating transcription, crystallization of the kinase-recruitment domain of RsbU in a form suitable for high-resolution structure determination is reported.
枯草芽孢杆菌的一般应激反应为其提供了对多种压力的保护性抗性。关键分子是RNA聚合酶的一个亚基，即σ(B)，它赋予启动子特异性并受两个信号模块调控。每个模块都包含蛋白激酶和磷酸酶以及激酶和磷酸酶的“开关”蛋白底物。开关分子的磷酸化状态间接控制σ(B)的活性。激酶RsbT与磷酸酶RsbU的结合刺激了其对底物磷酸化RsbV的酶活性。为了了解这些酶如何相互作用从而调控转录，本文报道了适合高分辨率结构测定的RsbU激酶招募结构域的晶体化情况。
