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The Saccharomyces cerevisiae Prp5 Protein Has RNA-dependent ATPase Activity with Specificity for U2 Small Nuclear RNA

O'Day, Christine L. and Dalbadie-McFarland, Gloria and Abelson, John (1996) The Saccharomyces cerevisiae Prp5 Protein Has RNA-dependent ATPase Activity with Specificity for U2 Small Nuclear RNA. Journal of Biological Chemistry, 271 (52). pp. 33261-33267. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:ODAjbc96

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Abstract

The Saccharomyces cerevisiae protein Prp5 is a member of the "DEAD box" family of putative RNA-dependent ATPases and helicases. The protein was purified from Escherichia coli and determined to be an RNA-dependent ATPase. The ATPase activity is 7-fold more specific for full-length U2 than for any of the other small nuclear RNAs or nonspecific RNAs tested. An RNaseH assay in extracts was used to demonstrate that Prp5 mediates an ATP-dependent conformational change in the intact U2 small nuclear ribonucleoprotein. We propose that this conformational change makes the branch point pairing sequence of U2 RNA accessible for pairing with the intron allowing formation of the pre-spliceosome.


Item Type:Article
Additional Information:©1996 by The American Society for Biochemistry and Molecular Biology, Inc. (Received for publication, May 1, 1996, and in revised form, September 10, 1996) We thank Drs. David McPheeters and David Horowitz for helpful discussion and suggestions. This work was supported by Grant GM32637 from the National Institutes of Health. 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.
Record Number:CaltechAUTHORS:ODAjbc96
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:ODAjbc96
Alternative URL:http://www.jbc.org/cgi/content/abstract/271/52/33261
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ID Code:5811
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:05 Jan 2007
Last Modified:26 Dec 2012 09:15

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