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Peculiarities in Activation of Hydrolytic Activity of Elongation Factors

机译:激活伸长因子水解活性的特性

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Translational GTPases (trGTPases) belong to the family of G proteins and play key roles at all stages of protein biosynthesis on the ribosome. Unidirectional and cyclic functioning of G proteins is ensured by their ability to switch between the active and inactive states due to GTP hydrolysis accelerated by the auxiliary GTPase-activating proteins. Although trGTPases interact with the ribosomes in different conformational states, they bind to the same conserved region, which, unlike in classical GTPase-activating proteins, is represented by ribosomal RNA. The resulting catalytic sites have almost identical structure in all elongation factors suggesting a common mechanism of GTP hydrolysis. However, fine details of the activated state formation and significantly different rates of GTP hydrolysis indicate the existence of distinctive features upon GTP hydrolysis catalyzed by the different factors. Here, we present a contemporary view on the mechanism of GTPase activation and GTP hydrolysis by the elongation factors EF-Tu, EF-G, and SelB based on the analysis of structural, biochemical, and bioinformatics data.
机译:翻译GTP酶(TRGTP酶)属于G蛋白的家族,并在核糖体上的蛋白质生物合成的所有阶段发挥关键作用。通过通过助剂GTP酶活化蛋白加速的GTP水解,通过它们在活性和无活性状态之间切换的能力来确保G蛋白的单向和环状功能。虽然TRGPASE与不同构象状态相互作用,但它们与相同的保守区域结合,其与典型GTP酶活化蛋白不同,其与核糖体RNA表示。所得催化位点在所有伸长因子中具有几乎相同的结构,表明GTP水解的常见机制。然而,活化状态形成的细节和GTP水解的显着不同的速率表明,在由不同因素催化的GTP水解时存在独特特征。在这里,我们基于结构,生物化学和生物信息学数据的分析,延长因子EF-TU,EF-G和SELB的GTP酶活化和GTP水解机制的现代观点。

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