Thermostability of Multidomain Proteins Studied by Domain Swapping between Mesophilic-Escherichia coli and Thermophilic-Bacillus stearothermophilus Elongation Factors EF-Tu

0191683 - UMG-J 20033198 RIV RU eng C - Conference Paper (international conference)
Jonák, Jiří - Šanderová, Hana - Maloň, Petr - Hůlková, Marta
Thermostability of Multidomain Proteins Studied by Domain Swapping between Mesophilic-Escherichia coli and Thermophilic-Bacillus stearothermophilus Elongation Factors EF-Tu.
Program of The Sixth International Engelhardt Conference on Molecular Biology. Moscow: Engelhardt Institute of Molecular Biology, 2003, s. 4.
[International Engelhardt Conference on Molecular Biology /6./. St. Peterburg - Moscow (RU), 29.06.2003-05.07.2003]
R&D Projects: GA ČR GA303/02/0689; GA AV ČR IAA5052206
Institutional research plan: CEZ:AV0Z4055905; CEZ:AV0Z5052915
Keywords : elongation factor EF-Tu, chimeric protein, thermostability
Subject RIV: EB - Genetics ; Molecular Biology

EF-Tu from moderately thermostable G+ bacterium Bacillus stearothermophilus, growing at around 60 0C, was chosen to determine how its overall thermostability is built from the contribution of individual protein domains and what makes this protein more thermostable than EF-Tu from mesophilic Escherichia coli (growing at 37 0C). For this purpose chimaeric forms of EF-Tu composed of domains of the mesophilic and thermophilic EF-Tus were constructed and their activity and thermostability compared with those of intact EF-Tus and their isolated G-domains.
Permanent Link: http://hdl.handle.net/11104/0087421