Počet záznamů: 1

The N-terminal region is crucial for the thermostability of the G-domain of Bacillus stearothermophilus EF-Tu

  1. 1.
    0335710 - UMG-J 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
    Grant CEP: GA AV ČR KJB500520601; GA MZd NR9138; GA MŠk 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

    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