Identification and Characterization of a Putative Arginine Kinase Homolog from Myxococcus xanthus Required for Fruiting Body Formation and Cell Differentiation
Identification and Characterization of a Putative Arginine Kinase Homolog from Myxococcus xanthus Required for Fruiting Body Formation and Cell Differentiation
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DOI：
10.1128/jb.06435-11
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发表时间：
2012-05-01
影响因子：
3.2
通讯作者：
Singer, Mitchell
中科院分区：
文献类型：
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作者：
Bragg, Jonathan;Rajkovic, Andrei;Singer, Mitchell
精氨酸激酶催化高能磷酸基从ATP到l -精氨酸的可逆转移，形成磷酸甘氨酸，在昆虫、甲壳类动物和一些单细胞生物中用作能量缓冲。它在脊椎动物中起着与磷酸肌酸类似的作用。最近，在几种细菌中发现了假定的精氨酸激酶，包括社会性革兰氏阴性土壤细菌粘球菌。目前还不清楚这些蛋白质在细菌中扮演什么角色，以及它们是否已经进化到在它们被发现的物种中获得新的功能。在这项研究中，我们对一种假定的M. xanthus精氨酸激酶Ark进行了生化纯化和表征，并证明它保留了通过ATP催化精氨酸磷酸化的能力。我们还在方舟基因中构建了一个零突变，并证明了它在某些应激反应和发育中的作用。
Arginine kinases catalyze the reversible transfer of a high-energy phosphoryl group from ATP to L-arginine to form phosphoarginine, which is used as an energy buffer in insects, crustaceans, and some unicellular organisms. It plays an analogous role to that of phosphocreatine in vertebrates. Recently, putative arginine kinases were identified in several bacterial species, including the social Gram-negative soil bacterium Myxococcus xanthus. It is still unclear what role these proteins play in bacteria and whether they have evolved to acquire novel functions in the species in which they are found. In this study, we biochemically purified and characterized a putative M. xanthus arginine kinase, Ark, and demonstrated that it has retained the ability to catalyze the phosphorylation of arginine by using ATP. We also constructed a null mutation in the ark gene and demonstrated its role in both certain stress responses and development.