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M109553200v1
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Papers In Press, published online ahead of print April 1, 2002
J. Biol. Chem, 10.1074/jbc.M109553200
Submitted on October 3, 2001
Revised on March 25, 2002
Accepted on March 29, 2002

Probing interactions between the U2 snRNP and the DEAD-box protein, Prp5

Barham K. Abu Dayyeh, Tiffani K. Quan, Marygrace A. Castro, and Stephanie W. Ruby

Molecular Genetics and Microbiology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico 87131

Corresponding Author: sruby{at}unm.edu

Pre-mRNA binding to the yeast U2 snRNP during prespliceosome formation requires ATP hydrolysis, the pre-mRNA’s highly conserved UACUAAC box of the branchpoint region, and several factors. Here we analyzed the binding of a radiolabeled 2’-Omethyl oligonucleotide (2’Ome oligo) complementary to U2 snRNA to study interactions between the UACUAAC box, U2 snRNP, and Prp5p, a DEAD-box protein necessary for prespliceosome formation. Binding of the 2’Ome oligo to the U2 snRNP in yeast cell extract was assayed by gel electrophoresis. Binding was rapid, enhanced by ATP, and dependent on U2 snRNP’s integrity and conformation. It was also stimulated by Prp5p which was found to physically associate with U2 snRNP. In vitro heat-inactivation of the Ts prp5-1 mutant extract decreased oligo binding to U2 and the ATP enhancement of binding by 3-fold. Furthermore, the Ts prp5-1 mutation mapped to the ATP-binding motif I within the helicase-like domain. Thus the catalytic activity of Prp5p likely promotes a conformational change in the U2 snRNP.


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