PMID:16081328
| Citation |
Sanderová, H and Jonák, J (2005) Opposite roles of domains 2+3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity. Biochim. Biophys. Acta 1752:11-7 |
|---|---|
| Abstract |
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 alpha-helical regions of the G-domain as revealed by CD spectroscopy. |
| Links |
PubMed Online version:10.1016/j.bbapap.2005.06.011 |
| Keywords |
Escherichia coli/genetics; GTP Phosphohydrolases/metabolism; Geobacillus stearothermophilus/genetics; Kinetics; Peptide Elongation Factor Tu/chemistry; Peptide Elongation Factor Tu/metabolism; Protein Denaturation; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/metabolism; Species Specificity; Thermodynamics |
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