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Originally published In Press as doi:10.1074/jbc.M200182200 on January 31, 2002

J. Biol. Chem., Vol. 277, Issue 15, 12810-12815, April 12, 2002
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The ATPase, RNA Unwinding, and RNA Binding Activities of Recombinant p68 RNA Helicase*

Youliang Huang and Zhi-Ren LiuDagger

From the Program in Cell and Molecular Biosciences, Department of Animal and Dairy Sciences, Auburn University, Auburn, Alabama 36849

p68 RNA helicase, a nuclear RNA helicase, was identified 2 decades ago. The protein plays very important roles in cell development and organ maturation. However, the biological functions and enzymology of p68 RNA helicase are not well characterized. We report the expression and purification of recombinant p68 RNA helicase in a bacterial system. The recombinant p68 is an ATP-dependent RNA helicase. ATPase assays demonstrated that double-stranded RNA (dsRNA) is much more effective than single-stranded RNA in stimulating ATP hydrolysis by the recombinant protein. Consistently, RNA-binding assays showed that p68 RNA helicase binds single-stranded RNA weakly in an ATP-dependent manner. On the other hand, the recombinant protein has very high affinity for dsRNA. Binding of the protein to dsRNA is ATP-independent. The data indicate that p68 may directly target dsRNA as its natural substrate. Interestingly, the recombinant p68 RNA helicase unwinds dsRNA in both 3' right-arrow 5' and 5' right-arrow 3' directions. This is the second example of a Asp-Glu-Ala-Asp (DEAD) box RNA helicase that unwinds RNA duplexes in a bi-directional manner.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: 210 Upchurch Hall, Auburn University, Auburn, AL 36849. E-mail: zrliu@acesag.auburn.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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