Microcalorimetric study of elongation factor Tu from Thermus thermophilus in nucleotide-free,GDP and GTP forms and in the presence of elongation factor Ts |
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Authors: | Sedlák Erik Sprinzl Mathias Grillenbeck Norbert Antalík Marián |
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Institution: | Department of Biochemistry, Faculty of Science P.J. Safárik University, Kosice, Slovakia. sedlak_er@saske.sk |
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Abstract: | Elongation factor (EF) Tu undergoes profound nucleotide-dependent conformational changes in its functional cycle. The thermodynamic parameters of the different Thermus thermophilus EF-Tu forms, its domains I, II/III and III, were determined by microcalorimetry. Thermal transitions of the EF-Tu.GDP and EF-Tu.guanosine-5'-beta,gamma-imido]triphosphate have a cooperative two-state character. Nucleotide removal affected the cooperativity of the thermal transition of EF-Tu. Microcalorimetric measurements of nucleotide-free EF-Tu and its separated domains showed that domains II/III have the main stabilizing role for the whole protein. Despite the fact that strong interactions between elongation factors Tu and Ts from T. thermophilus at 20 degrees C exist, the thermal transition of neither protein in the complex was significantly affected. |
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