The DEAD Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis
The DEAD Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis
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DOI：
10.1021/bi901278p
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发表时间：
2009-11-17
期刊：
影响因子：
2.9
通讯作者：
Klostermeier, Dagmar
中科院分区：
文献类型：
--
作者：
Aregger, Regula;Klostermeier, Dagmar
DEAD box解旋酶以ATP水解为代价解开RNA双链体。最近，解旋已被证明在没有ATP水解。在这里，我们表明，ADP。BeFx通过YxiN支持RNA解旋，YxiN是一种特异性识别23S rRNA中发夹的DEAD盒解旋酶。ADP-AlFx和ADP. MgFx不促进RNA解旋，但所有ATP类似物诱导解旋酶核心的闭合构象，如RNA解旋所需。我们的研究结果表明，在解旋酶核心的域间裂缝关闭后，ATP结合在周期的开始。再开放发生在ATP水解后，最有可能与磷酸盐释放相结合。
DEAD box helicases unwind RNA duplexes at the expense of ATP hydrolysis. Recently, unwinding has been demonstrated in the absence of ATP hydrolysis. Herein, we show that ADP . BeFx supports RNA unwinding by YxiN, a DEAD box helicase that specifically recognizes a hairpin in 23S rRNA. ADP-AlFx and ADP.MgFx do not promote RNA unwinding, but all ATP analogues induce a closed conformation of the helicase core as required for RNA unwinding. Our results show that the interdomain cleft in the helicase core closes upon ATP binding at the beginning of the cycle. Reopening occurs after ATP hydrolysis, most likely coupled to phosphate release.