Bubunenko M G, Gudkov A T
Institute of Protein Research, Academy of Sciences of the USSR, Pushchino, Moscow Region.
Biomed Sci. 1990 Feb;1(2):127-32.
Limited trypsinolysis was used to study conformational changes in elongation factors Tu and G. The trypsin cleavage rates of the factors differed and depended on both their interaction with ligands and the presence or absence of ribosomes. When the factors were bound to ribosomes, changes in their sensitivity to trypsin were observed depending on whether GDP or GTP was present in the complex, i.e. on the hydrolysis state of the guanine nucleotide ligand. The possible significance of factor structural changes for their functioning is discussed.
采用有限胰蛋白酶水解法研究延伸因子Tu和G的构象变化。这两种因子的胰蛋白酶切割速率不同，且取决于它们与配体的相互作用以及核糖体的存在与否。当这些因子与核糖体结合时，根据复合物中存在的是GDP还是GTP，即鸟嘌呤核苷酸配体的水解状态，可观察到它们对胰蛋白酶敏感性的变化。文中讨论了因子结构变化对其功能的可能意义。
