The cation-dependent G-proteins: In a class of their own

被引：32

作者：

Ash, Miriam-Rose ^{[1
]}

Maher, Megan J. ^{[2
]}

Guss, J. Mitchell ^{[1
]}

Jormakka, Mika ^{[3
]}

机构：

[1] Univ Sydney, Sch Mol Biosci, Sydney, NSW 2006, Australia

[2] La Trobe Univ, La Trobe Inst Mol Sci, Melbourne, Vic, Australia

[3] Univ Sydney, Sydney Med Sch, Sydney, NSW 2006, Australia

来源：

FEBS LETTERS | 2012年 / 586卷 / 16期

基金：

英国医学研究理事会;

关键词：

Cation-dependent GTPase; Potassium stimulation; GTPase activation; G-protein classification; Ribosome-assembly GTPase; Dynamin-like GTPase; GTP-BINDING PROTEIN; 50-S RIBOSOMAL-SUBUNIT; BACILLUS-SUBTILIS; ESCHERICHIA-COLI; SULFOLOBUS-SOLFATARICUS; CATALYTIC MACHINERY; THERMOTOGA-MARITIMA; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; UPTAKE SYSTEM;

D O I：

10.1016/j.febslet.2012.06.030

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2218 / 2224

页数：7

共 54 条

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