当EF-G与核糖体相互作用时，L7/L12蛋白会改变其构象。
The L7/L12 proteins change their conformation upon interaction of EF-G with ribosomes.
作者信息
Gudkov A T, Gongadze G M
出版信息
FEBS Lett. 1984 Oct 15;176(1):32-6. doi: 10.1016/0014-5793(84)80906-0.
PMID:6092137
Abstract
The different functional complexes of ribosomes with elongation factor F (EF-G) were studied by digestion experiments with trypsin. It was found that upon interaction of EF-G with ribosomes the L7/L12 proteins are sensitive to trypsin and are trypsin resistant after dissociation of EF-G from ribosomes. The significance of conformational alterations in the L7/L12 and also in the other proteins in the translation process is discussed.
摘要
通过用胰蛋白酶进行消化实验，研究了核糖体与延伸因子F（EF-G）的不同功能复合物。结果发现，当EF-G与核糖体相互作用时，L7/L12蛋白对胰蛋白酶敏感，而在EF-G从核糖体解离后则对胰蛋白酶具有抗性。文中讨论了L7/L12以及翻译过程中其他蛋白质构象改变的意义。
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