Structural basis for the function of DEAH helicases
Structural basis for the function of DEAH helicases
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DOI：
10.1038/embor.2010.11
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发表时间：
2010-03-01
期刊：
影响因子：
7.7
通讯作者：
Nielsen, Klaus H.
中科院分区：
文献类型：
--
作者：
He, Yangzi;Andersen, Gregers R.;Nielsen, Klaus H.
DEH解旋酶参与前信使RNA的剪接和核糖体的生物发生。酵母Prp43P-ADP的结构揭示了Deah解旋酶与DNA解旋酶的同源性，并存在一个寡核苷酸结合基序。来自第二RecA结构域的β-发夹夹在两个羧基末端结构域之间，并阻断对由RecA结构域和C-末端结构域形成的封闭的RNA结合位点的访问。ATP结合和水解可能会导致发夹的构象变化，这对RNA解离或核糖核蛋白重塑是重要的。Prp43p的结构为所有Deah解旋酶的功能和遗传分析提供了框架。
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 carboxyterminal 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.