Previous Article | Next Article ![]()
Journal of Bacteriology, December 2000, p. 7078-7082, Vol. 182, No. 24
Department of Biochemistry, Robert Wood
Johnson Medical School, Piscataway, New Jersey 08854
Received 19 May 2000/Accepted 7 August 2000
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. Km and
kcat at 70°C were 833 µM and 9.3 min
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Characterization of GTPase Activity of TrmE, a
Member of a Novel GTPase Superfamily, from Thermotoga
maritima
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.
*
Corresponding author. Mailing address: Department of
Biochemistry, Robert Wood Johnson Medical School, 675 Hoes Ln.,
Piscataway, NJ 08854. Phone: (732) 235-4115. Fax: (732) 235-4559. E-mail: inouye{at}umdnj.edu.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»