0335710 - ÚMG 2010 RIV NL eng J - Článek v odborném periodiku
Šanderová, Hana - Tišerová, Hana - Barvík, I. - Sojka, Luděk - Jonák, Jiří - Krásný, Libor
The N-terminal region is crucial for the thermostability of the G-domain of Bacillus stearothermophilus EF-Tu.
Biochimica Et Biophysica Acta-Proteins and Proteomics. Roč. 1804, č. 1 (2010), s. 147-155. ISSN 1570-9639. E-ISSN 1878-1454
Grant CEP: GA AV ČR KJB500520601; GA MZd NR9138; GA MŠMT 2B06065
Výzkumný záměr: CEZ:AV0Z50520514
Klíčová slova: thermostability * G protein * EF-Tu * G-domain * Bacillus
Kód oboru RIV: EB - Genetika a molekulární biologie
Impakt faktor: 2.773, rok: 2010 ; AIS: 0.96, rok: 2010
DOI: https://doi.org/10.1016/j.bbapap.2009.09.024

Bacterial elongation factor Tu (EF-Tu) is a model monomeric G protein composed of 3 covalently linked domains. Previously, we evaluated the contributions of individual domains to the thermostability of EF-Tu from thermophilic bacterium Bacillus stearothermophilus. We showed that domain 1 (G-domain) sets up the basal level of thermostability for the whole protein. Here we located the thermostability determinants distinguishing the thermophilic domain 1 from mesophilic domain 1. By systematically swapping protein regions differing between G-domains from mesophilic B. subtilis and thermophilic B. stearothermophilus we demonstrate that a small portion of the protein, the N-terminal 12 aa residues, plays a key role in the thermostability of this domain. The thermostabilizing effect of the N-terminal region could be mediated by stabilizing the functionally important effector region and the effect of the N-terminal region is significant also for the thermostability of full-length EF-Tu.
Trvalý link: http://hdl.handle.net/11104/0180101