首页> 美国卫生研究院文献>Journal of Bacteriology >Fancy meeting you here! A fresh look at prokaryotic protein phosphorylation.
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Fancy meeting you here! A fresh look at prokaryotic protein phosphorylation.

机译:想在这里见到你!对原核蛋白磷酸化的重新审视。

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摘要

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.
机译:细菌是各种蛋白质磷酸化-去磷酸化系统的宿主(图1)。早在五年前,已知的系统就被认为是新兴的并且绝对是原核生物特有的。今天,我们知道大多数蛋白激酶和蛋白磷酸酶均来自一组常见且可能很古老的原型。原核生物和真核生物特异的蛋白激酶和蛋白磷酸酶很少见,代表例外,并非以前认为的规则。共有性表明,动态的,通用的调节机制首先要早于适应蛋白质功能的调节,甚至早于诸如变构等的更多“基本”机制。常见的分子主题的存在证实了微生物世界提供了独特的,尚未开发的库以及用于理解对所有生物至关重要的调控机制的功能强大的工具集,这些工具的多样性和实验可塑性将为探索和理解细胞调控的关键模式提供新途径。

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