The Bacillus subtilis RNA helicase YxiN is distended in solution
The Bacillus subtilis RNA helicase YxiN is distended in solution
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DOI：
10.1529/biophysj.107.120709
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发表时间：
2008-01-01
影响因子：
3.4
通讯作者：
Mckay, David B.
中科院分区：
文献类型：
--
作者：
Wang, Shuying;Overgaard, Michael T.;Mckay, David B.
枯草芽孢杆菌YxiN蛋白是DEX（D/H）-盒蛋白家族的模块化三结构域RNA解旋酶。前两个结构域形成高度保守的解旋酶核心，第三个结构域赋予RNA靶结合特异性。小角度X-射线散射的YxiN和两个结构域的片段显示，该蛋白质在溶液中有一个膨胀的结构，在复制过程中涉及的解旋酶。这些数据与分子伴侣活性一致，其中YxiN的羧基末端结构域将蛋白质束缚在其靶标附近，并且解旋酶核心自由地与RNA双链体短暂相互作用，可能熔化二级结构的错误折叠元件。
The Bacillus subtilis YxiN protein is a modular three-domain RNA helicase of the DEx(D/H)-box protein family. The first two domains form the highly conserved helicase core, and the third domain confers RNA target binding specificity. Small angle x-ray scattering on YxiN and two-domain fragments thereof shows that the protein has a distended structure in solution, in contrast to helicases involved in replication processes. These data are consistent with a chaperone activity in which the carboxy-terminal domain of YxiN tethers the protein to the vicinity of its targets and the helicase core is free to transiently interact with RNA duplexes, possibly to melt out misfolded elements of secondary structure.