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RH70, a bidirectional RNA helicase, co-purifies with U1snRNP
1Department of Biochemistry and Molecular Biology, Graduate School of Biomedical Sciences, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103, USA. leecg@umdnj.edu
The Journal of Biological Chemistry
|August 24, 2002
Summary
This study identifies a novel RNA helicase (RH70), also known as DDX17, that unwinds RNA in an ATP-dependent manner. Its association with U1snRNP suggests a role in early pre-mRNA splicing.
Area of Science:
- Molecular Biology
- Biochemistry
Background:
- U1 small nuclear ribonucleoprotein particle (U1snRNP) is crucial for pre-mRNA splicing.
- RNA helicases play vital roles in RNA metabolism, including splicing.
Purpose of the Study:
- To identify and characterize a novel RNA helicase associated with U1snRNP.
- To elucidate the biochemical properties and potential function of this RNA helicase in splicing.
Main Methods:
- Co-purification of RNA helicase (RH70) and U1snRNP.
- Peptide sequence analysis using mass spectrometry and Edman degradation.
- Biochemical assays to determine RNA helicase and ATPase activities.
Main Results:
- RH70 was identified as DDX17, a 70-kDa RNA helicase.
- RH70/DDX17 unwinds duplex RNA, but not DNA, in an ATP-dependent manner.
- The enzyme exhibits high specificity for ATP and unwinds RNA with single-stranded regions.
Conclusions:
- RH70/DDX17's association with U1snRNP and its RNA unwinding activity suggest a role in pre-mRNA splicing.
- The helicase likely functions in the early stages of splicing involving U1snRNP.
- This finding provides new insights into the molecular mechanisms of splicing regulation.