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A more recent version of this article appeared on October 11, 2002
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C200337200v1
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Papers In Press, published online ahead of print August 21, 2002
J. Biol. Chem, 10.1074/jbc.C200337200
Submitted on June 3, 2002
Revised on June 27, 2002
Accepted on August 21, 2002

RH70, a bidirectional RNA helicase, co-purifies with U1snRNP

Chee-Gun Lee

Department of Biochemistry and Molecular Biology, UMDNJ-New Jersey Medical School, Newark, NJ 07103

Corresponding Author: leecg{at}umdnj.edu

In this report, I describe the co-purification of a novel 70 kDa RNA helicase (RH701) and U1snRNP through 6 column steps. Peptide sequence analysis by mass spectrometry and Edman degradation revealed that RH70 is the previously reported DDX17. Biochemical characterization of RH70, obtained by partial separation from U1snRNP, yielded the following results. (a) RH70 mediates the unwinding of duplex RNA but not DNA in an ATP-dependent manner. (b) Both the RNA-dependent ATPase and RNA helicase activities of RH70 are highly specific for ATP, exhibiting an apparent Km of 0.5 mM. (c) RH70 catalyzes the unwinding of duplex RNA containing single-stranded (ss) regions at either the 5'-end or the 3'-end. Its association with U1snRNP and ATP specificity suggest a role for RH70 in pre-mRNA splicing, in particular, at the early stages of the splicing reaction involving U1snRNP.


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