Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.
Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.
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DOI：
10.1093/nar/gkp1118
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发表时间：
2010-03
影响因子：
14.9
通讯作者：
Cameron CE
中科院分区：
文献类型：
--
作者：
Wang Q;Arnold JJ;Uchida A;Raney KD;Cameron CE
RNA helicases function in numerous aspects of RNA biology. These enzymes are RNA-stimulated ATPases that translocate on RNA and unwind or remodel structured RNA in an ATP-dependent fashion. How ATP and the ATPase cycle fuel the work performed by helicases is not completely clear. The hepatitis C virus RNA helicase, NS3, is an important model system for this class of enzymes. NS3 binding to a single-/double-strand RNA or DNA junction leads to ATP-independent melting of the duplex and formation of a complex capable of ATP-dependent unwinding by using a spring-loaded mechanism. We have established an RNA substrate for NS3 that can be unwound in a single sub-step. Our studies are consistent with a model in which a single ATP binding and/or hydrolysis event sets the unwinding spring and phosphate dissociation contributes to release of the spring, thereby driving the power stroke used for unwinding.
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