The cation-dependent G-proteins: In a class of their own
The cation-dependent G-proteins: In a class of their own
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DOI：
10.1016/j.febslet.2012.06.030
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发表时间：
2012-07-30
期刊：
影响因子：
3.5
通讯作者：
Jormakka, Mika
中科院分区：
文献类型：
--
作者：
Ash, Miriam-Rose;Maher, Megan J.;Jormakka, Mika
G-蛋白是一些最重要和最丰富的酶，但其固有的核苷酸水解反应是出了名的缓慢，必须在体内加速。最近关于参与核糖体组装的动力蛋白和GTP酶的实验表明，它们的水解性受到钾离子的刺激。本文提出的假设是，阳离子介导的G-蛋白的激活比目前所认识的更常见，并且这种GTP酶代表了一类结构和功能上独特的G-蛋白。基于序列分析，我们提供了一个预测的阳离子依赖的GTP酶列表，它几乎涵盖了TES、Obg-HflX、YqeH-like和Dynamin超家族的所有成员。这一分析的结果有效地重新定义了许多这些G蛋白应该在体外研究的条件。(C)2012年欧洲生化学会联合会。爱思唯尔出版，版权所有。
G-proteins are some of the most important and abundant enzymes, yet their intrinsic nucleotide hydrolysis reaction is notoriously slow and must be accelerated in vivo. Recent experiments on dynamin and GTPases involved in ribosome assembly have demonstrated that their hydrolysis activities are stimulated by potassium ions. This article presents the hypothesis that cation-mediated activation of G-proteins is more common than currently realised, and that such GTPases represent a structurally and functionally unique class of G-proteins. Based on sequence analysis we provide a list of predicted cation-dependent GTPases, which encompasses almost all members of the TEES, Obg-HflX, YqeH-like and dynamin superfamilies. The results from this analysis effectively re-define the conditions under which many of these G-proteins should be studied in vitro. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.