The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase
The Elongator subcomplex Elp456 is a hexameric RecA-like ATPase
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DOI：
10.1038/nsmb.2234
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发表时间：
2012-03-01
影响因子：
16.8
通讯作者：
Mueller, Christoph W.
中科院分区：
文献类型：
--
作者：
Glatt, Sebastian;Letoquart, Juliette;Mueller, Christoph W.
Elongator最初被描述为一种RNA聚合酶II相关因子，但后来被认为与广泛的细胞活动有关。由于其在某些神经退行性疾病中的作用，它也引起了临床关注。在这里，我们描述的延伸蛋白4，5和6（Elp456）的酿酒酵母亚复合物的晶体结构。每个亚基显示几乎相同的RecA折叠，形成类似六聚体RecA样ATP酶的异六聚体环状结构。这一结构发现得到了不同的体外和体内互补方法的支持，包括六聚体Elp456亚复合物以ATP调节的方式与tRNA的特异性结合。我们的研究结果支持的作用，延伸在tRNA修饰，解释每个Elp4，Elp5和Elp6亚基的复杂的完整性的重要性，并提出了一个模型的整体架构的全息延伸复杂。
Elongator was initially described as an RNA polymerase II-associated factor but has since been associated with a broad range of cellular activities. It has also attracted clinical attention because of its role in certain neurodegenerative diseases. Here we describe the crystal structure of the Saccharomyces cerevisiae subcomplex of Elongator proteins 4, 5 and 6 (Elp456). The subunits each show almost identical RecA folds that form a heterohexameric ring-like structure resembling hexameric RecA-like ATPases. This structural finding is supported by different complementary in vitro and in vivo approaches, including the specific binding of the hexameric Elp456 subcomplex to tRNAs in a manner regulated by ATP. Our results support a role of Elongator in tRNA modification, explain the importance of each of the Elp4, Elp5 and Elp6 subunits for complex integrity and suggest a model for the overall architecture of the holo-Elongator complex.