DEAH 解旋酶功能的结构基础。
Structural basis for the function of DEAH helicases.
机构信息
Department of Molecular Biology, Aarhus University, Aarhus, Denmark.
出版信息
EMBO Rep. 2010 Mar;11(3):180-6. doi: 10.1038/embor.2010.11. Epub 2010 Feb 19.
Abstract
DEAH helicases participate in pre-messenger RNA splicing and ribosome biogenesis. The structure of yeast Prp43p-ADP reveals the homology of DEAH helicases to DNA helicases and the presence of an oligonucleotide-binding motif. A beta-hairpin from the second RecA domain is wedged between two carboxy-terminal domains and blocks access to the occluded RNA binding site formed by the RecA domains and a C-terminal domain. ATP binding and hydrolysis are likely to induce conformational changes in the hairpin that are important for RNA unwinding or ribonucleoprotein remodelling. The structure of Prp43p provides the framework for functional and genetic analysis of all DEAH helicases.
摘要
DEAH 解旋酶参与前信使 RNA 剪接和核糖体生物发生。酵母 Prp43p-ADP 的结构揭示了 DEAH 解旋酶与 DNA 解旋酶的同源性以及寡核苷酸结合基序的存在。第二个 RecA 结构域中的β发夹楔入两个羧基末端结构域之间，并阻止了由 RecA 结构域和 C 末端结构域形成的封闭 RNA 结合位点的进入。ATP 结合和水解可能会诱导发夹的构象变化，这对于 RNA 解旋或核糖核蛋白重塑很重要。Prp43p 的结构为所有 DEAH 解旋酶的功能和遗传分析提供了框架。
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