延伸因子G的精氨酸29和59对于核糖体上的GTP水解或转位很重要。
Arginines 29 and 59 of elongation factor G are important for GTP hydrolysis or translocation on the ribosome.
作者信息
Mohr D, Wintermeyer W, Rodnina M V
机构信息
Institutes of Physical Biochemistry and Molecular Biology, University of Witten/Herdecke, 58448 Witten, Germany.
出版信息
EMBO J. 2000 Jul 3;19(13):3458-64. doi: 10.1093/emboj/19.13.3458.
Abstract
GTP hydrolysis by elongation factor G (EF-G) is essential for the translocation step in protein elongation. The low intrinsic GTPase activity of EF-G is strongly stimulated by the ribosome. Here we show that a conserved arginine, R29, of Escherichia coli EF-G is crucial for GTP hydrolysis on the ribosome, but not for GTP binding or ribosome interaction, suggesting that it may be directly involved in catalysis. Another conserved arginine, R59, which is homologous to the catalytic arginine of G(alpha) proteins, is not essential for GTP hydrolysis, but influences ribosome binding and translocation. These results indicate that EF-G is similar to other GTPases in that an arginine residue is required for GTP hydrolysis, although the structural changes leading to GTPase activation are different.
摘要
延伸因子G（EF-G）催化的GTP水解对于蛋白质延伸过程中的转位步骤至关重要。核糖体可强烈刺激EF-G较低的内在GTP酶活性。我们在此表明，大肠杆菌EF-G中一个保守的精氨酸R29对于核糖体上的GTP水解至关重要，但对于GTP结合或核糖体相互作用并非如此，这表明它可能直接参与催化作用。另一个保守的精氨酸R59与Gα蛋白的催化精氨酸同源，对于GTP水解并非必需，但会影响核糖体结合和转位。这些结果表明，EF-G与其他GTP酶相似，即GTP水解需要一个精氨酸残基，尽管导致GTP酶激活的结构变化有所不同。
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