Opposite roles of domains 2+3 of Escherichia coli EF-Tu nd Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity
1.
SYSNO ASEP
0025248
Druh ASEP
J - Článek v odborném periodiku
Zařazení RIV
J - Článek v odborném periodiku
Poddruh J
Ostatní články
Název
Opposite roles of domains 2+3 of Escherichia coli EF-Tu nd Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity
Překlad názvu
Opačný vliv domén 2+3 z EF-Tu z Escherichia coli a Bacillus stearothermophilus na regulaci GTPázové aktivity EF-Tu
Tvůrce(i)
Šanderová, Hana (UMG-J) Jonák, Jiří (UMG-J)
Zdroj.dok.
Biochimica Et Biophysica Acta-Proteins and Proteomics. - : Elsevier
- ISSN 1570-9639
Roč. 1752, č. 1 (2005), s. 11-17
Poč.str.
7 s.
Jazyk dok.
eng - angličtina
Země vyd.
NL - Nizozemsko
Klíč. slova
elongation factor Tu ; GTPase regulation ; G-domain
Vědní obor RIV
EB - Genetika a molekulární biologie
CEP
GA303/02/0689 GA ČR - Grantová agentura ČR
CEZ
AV0Z50520514 - UMG-J (2005-2011)
Anotace
The effect of noncatalytic domains 2+3 on the intrinsic activity and thermostability of the EF-Tu GTPase center was evaluated in experiments with isolated domains 1 and six chimeric variants of mesophilic Escherichia coli (Ec) and thermophilic Bacillus stearothermophilus (Bst) EF-Tus. The isolated catalytic domains 1 of both EF-Tus displayed similar GTPase activities at their optimal temperatures. However, noncatalytic domains 2+3 of the EF-Tus influenced the GTPase activity of domains 1 differently, depending on the domain origin. Ecdomains 2+3 suppressed the GTPase activity of the Ecdomain 1, whereas those of BstEF-Tu stimulated the Bstdomain 1 GTPase. Domain 1 and domains 2+3 of both EF-Tus positively cooperated to heat-stabilize their GTPase centers to attain optimal activity at a temperature close to the optimal growth temperature of either organism. This can be explained by a stabilization effect of domains 2+3 on a-helical regions of the G-domain as revealed by CD spectroscopy.
