Characterization of GTPase activity of TrmE, a member of a novel GTPase super-family, from Thermotoga maritima

被引：42

作者：

Yamanaka, K ^{[1
]}

Hwang, JH ^{[1
]}

Inouye, M ^{[1
]}

机构：

[1] Robert Wood Johnson Med Sch, Dept Biochem, Piscataway, NJ 08854 USA

来源：

JOURNAL OF BACTERIOLOGY | 2000年 / 182卷 / 24期

关键词：

D O I：

10.1128/JB.182.24.7078-7082.2000

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A gene encoding a putative GTP-binding protein, a TrmE homologue that is highly conserved in both prokaryotes and eukaryotes, was cloned from Thermotoga maritima, a hyperthermophilic bacterium. T. maritima TrmE was overexpressed in Escherichia coli and purified. TrmE has a GTPase activity but no ATPase activity. The GTPase activity can be competed with GTP, GDP, and dGTP but not with GMP, ATP, CTP, or UTP, K-m and k(cat) at 70 degreesC were 833 muM and 9.3 min(-1), respectively. Our results indicate that TrmE is a GTP-binding protein with a very high intrinsic GTP hydrolysis rate. We also propose that TrmE homologues constitute a novel subfamily of the GTPase superfamily.

引用

页码：7078 / 7082

页数：5

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