CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis
CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis
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DOI：
10.1099/mic.0.022475-0
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发表时间：
2009-03-01
期刊：
影响因子：
2.8
通讯作者：
Seror, Simone J.
中科院分区：
文献类型：
--
作者：
Absalon, Cedric;Obuchowski, Michal;Seror, Simone J.
枯草芽孢杆菌中保守的prPC、prkC、cPGA基因分别编码丝氨酸/苏氨酸磷酸酶、同源感受器蛋白激酶(含有一个与肽聚糖前体结合的外部面团结构域)和CPGA，这是一种与形状决定和肽聚糖沉积有关的小核糖体相关GTP酶。在这项研究中，在寻找PrkC和PrPC靶标的过程中，我们发现，在体外，CPGA本身在丝氨酸和苏氨酸上被磷酸化，另一种GTP酶，翻译因子EF-Tu，也被保守的T384残基上的激酶磷酸化。两种底物都在体外被PrPC去磷酸化。此外，我们在体外和体内都发现了一种10.3 kDa的多肽YezB，它是应激体的一个组成部分，是这两种酶的底物。我们认为PrPC/PrkC/CPGA系统是参与协调枯草杆菌细胞壁扩张和生长的调控网络的重要组成部分。
The conserved prpC, prkC, cpgA locus in Bacillus subtilis encodes respectively a Ser/Thr phosphatase, the cognate sensor kinase (containing an external PASTA domain suggested to bind peptidoglycan precursors) and CpgA, a small ribosome-associated GTPase that we have shown previously is implicated in shape determination and peptidoglycan deposition. In this study, in a search for targets of PrkC and PrpC, we showed that, in vitro, CpgA itself is phosphorylated on serine and threonine, and another GTPase, the translation factor EF-Tu, is also phosphorylated by the kinase on the conserved T384 residue. Both substrates are dephosphorylated by PrpC in vitro. In addition, we identified YezB, a 10.3 kDa polypeptide, and a component of the stressosome, as a substrate for both enzymes in vitro and apparently in vivo. We propose that the PrpC/PrkC/CpgA system constitutes an important element of a regulatory network involved in the coordination of cell wall expansion and growth in B. subtilis.