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首页> 外文期刊>EMBO Journal >Structural and functional insights into the human Upf1 helicase core
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Structural and functional insights into the human Upf1 helicase core

机译：结构和功能的洞察人类Upf1解旋酶的核心

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摘要

Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that recognizes and degrades aberrant mRNAs containing premature stop codons. A critical protein in NMD is Upf1p, which belongs to the helicase super family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to promote transitions in the structure of RNA or RNA-protein complexes. The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural comparison combined with mutational analysis identifies a likely single-stranded RNA (ssRNA)-binding channel, and a cycle of conformational change coupled to ATP binding and hydrolysis. These conformational changes alter the likely ssRNA-binding channel in a manner that can explain how ATP binding destabilizes ssRNA binding to Upf1p.
机译：Nonsense-mediated mRNA衰变(NMD)是一个信使rna监测途径识别和降解异常的mrna包含过早停止密码子。Upf1p NMD的关键蛋白,属于解旋酶超家族1 (SF1),和认为利用ATP水解的能量促进RNA的结构或转换rna蛋白质复合物。人类的催化核心Upf1p决定三个州(磷酸盐、AMPPNP和ADP-bound形式)显示一个包含总体结构两个RecA-like域有两个额外的域的氨基RecA-like域。结合突变结构比较分析确定可能单链RNA(ssRNA)绑定频道,一个周期的与ATP绑定和构象变化的耦合水解。可能ssRNA-binding通道的方式可以解释ATP结合撼动ssRNA如何Upf1p绑定。

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