Novel substrates of Mycobacterium tuberculosis PknH Ser/Thr kinase

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• 作者：Xingji Zheng ; K.G. Papavinasasundaram ; Yossef Av-Gay
• 关键词：Ser/Thr kinase ; Mycobacterium tuberculosis ; TB ; Bioinformatics ; Activation loop
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2007
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：30 March 2007
• 卷：355
• 期：1
• 页码：162-168
• 文件大小：185 K

摘要

PknH Ser/Thr protein kinase of Mycobacterium tuberculosis controls the expression of a variety of cell wall related enzymes and regulates the in vivo growth in mice. Therefore, we predicted that the PknH kinase could phosphorylate several substrates controlling different metabolic and physiological pathways. Using a bioinformatic approach, we identified 40 potential substrates. Two substrates were shown to be phosphorylated by recombinant PknH kinase in vitro. Point mutation studies verified that substrates are phosphorylated at the in silico-predicted sites. Kinetic studies revealed a similar relative-phosphorylation rate (V_max) of PknH towards two new substrates and the only previously known substrate, EmbR. Unlike the EmbR protein, the Rv0681 and DacB1 proteins do not contain an FHA domain and are possible participants of new signaling pathways mediated by the PknH kinase in M. tuberculosis.