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Molecular and Cellular Biology, August 2002, p. 5443-5450, Vol. 22, No. 15
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.15.5443-5450.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

p68 RNA Helicase Is an Essential Human Splicing Factor That Acts at the U1 snRNA-5' Splice Site Duplex

Zhi-Ren Liu*

Program in Cell & Molecular Biosciences and Department of Animal Sciences, Auburn University, Auburn, Alabama 36849

Received 21 February 2002/ Returned for modification 8 April 2002/ Accepted 3 May 2002

Modulation of the interaction between U1 snRNP and the 5' splice site (5'ss) is a key event that governs 5'ss recognition and spliceosome assembly. Using the methylene blue-mediated cross-linking method (Z. R. Liu, A. M. Wilkie, M. J. Clemens, and C. W. Smith, RNA 2:611-621, 1996), a 65-kDa protein (p65) was shown to interact with the U1-5'ss duplex during spliceosome assembly (Z. R. Liu, B. Sargueil, and C. W. Smith, Mol. Cell. Biol. 18:6910-6920, 1998). In this report, p65 was identified as p68 RNA helicase and shown to be essential for in vitro pre-mRNA splicing. Depletion of endogenous p68 RNA helicase does not affect the loading of the U1 snRNP to the 5'ss during early stage of splicing. However, dissociation of the U1 from the 5'ss is largely inhibited. The data suggest that p68 RNA helicase functions in destabilizing the U1-5'ss interactions. Furthermore, depletion of p68 RNA helicase arrested spliceosome assembly at the prespliceosome stage, suggesting that p68 may play a role in the transition from prespliceosome to spliceosome.

* Mailing address: 210 Upchurch Hall, Auburn University, Auburn, AL 36849. Phone: (334) 844-1536. Fax: (334) 844-1519. E-mail: zrliu{at}acesag.auburn.edu.

Molecular and Cellular Biology, August 2002, p. 5443-5450, Vol. 22, No. 15
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.15.5443-5450.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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