Kennelly P J, Potts M
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA.
J Bacteriol. 1996 Aug;178(16):4759-64. doi: 10.1128/jb.178.16.4759-4764.1996.
Bacteria play host to a wide range of protein phosphorylation-dephosphorylation systems (Fig. 1). As little as five years ago the known systems were thought to be late-emerging and absolutely prokaryote specific. Today we know that most protein kinases and protein phosphatases are descended from a set of common, and possibly quite ancient, prototypes. Prokaryote- and eukaryote-specific protein kinases and protein phosphatases are rare and represent exceptions, not the rule as previously thought. Commonality suggests that a dynamic and versatile regulatory mechanism was first adapted to the modulation of protein function as early if not earlier than more "basic" mechanisms such as allosterism, etc. The existence of common molecular themes confirms that the microbial world offers a unique, largely untapped library and a powerful set of tools for the understanding of a regulatory mechanism which is crucial to all organisms, tools whose diversity and experimental malleability will provide new avenues for exploring and understanding key modes of cellular regulation.
细菌拥有多种蛋白质磷酸化 - 去磷酸化系统（图1）。就在仅仅五年前，已知的这些系统还被认为是后期出现的，并且绝对是原核生物特有的。如今我们知道，大多数蛋白激酶和蛋白磷酸酶都源自一组共同的、可能相当古老的原型。原核生物和真核生物特有的蛋白激酶和蛋白磷酸酶很少见，是例外情况，而非如之前所认为的那样是普遍规律。这种共性表明，一种动态且通用的调节机制最早即便不比变构等更“基本”的机制更早，也是在与它们相同的时期被用于调节蛋白质功能。共同分子主题的存在证实，微生物世界提供了一个独特的、很大程度上未被开发的文库以及一套强大的工具，用于理解对所有生物体都至关重要的一种调节机制，这些工具的多样性和实验可塑性将为探索和理解细胞调节的关键模式提供新途径。
