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J. Biol. Chem., Vol. 277, Issue 20, 17743-17750, May 17, 2002
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From the Department of Microbiology and Immunology, Weill Medical
College of Cornell University, New York, New York 10021
The essential Saccharomyces
cerevisiae PRP43 gene encodes a 767-amino acid protein of
the DEXH-box family. Prp43 has been implicated in
spliceosome disassembly (Arenas, J. E., and Abelson, J. N. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 11798-11802). Here we show that purified recombinant Prp43 is an
RNA-dependent ATPase. Alanine mutations at conserved
residues within motifs I (119GSGKT123), II
(215DEAH218) and VI
(423QRAGRAGR430) that diminished ATPase
activity in vitro were lethal in vivo, indicating that ATP hydrolysis is necessary for the biological function
of Prp43. Overexpression of lethal, ATPase-defective mutants in a
wild-type strain resulted in dominant-negative growth inhibition. The
ATPase-defective mutant T123A interfered in trans with the
in vitro splicing function of wild-type Prp43. T123A did
not affect the chemical steps of splicing or the release of mature
mRNA from the spliceosome, but it blocked the release of the
excised lariat-intron from the spliceosome. We show that the lariat-intron is not accessible to debranching by purified Dbr1 when it
is held in the T123A-arrested splicing complex. Our results define a
new ATP-dependent step of splicing that is catalyzed by Prp43.
Prp43 Is an Essential RNA-dependent ATPase Required
for Release of Lariat-Intron from the Spliceosome*
*
This work was supported by National Institutes of Health
Grant GM50288.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.
To whom correspondence should be addressed: Dept. of Microbiology
and Immunology, Weill Medical College of Cornell University, New York,
NY 10021. Tel.: 212-746-6518; Fax: 212-746-8587; E-mail: bschwer@mail.med.cornell.edu.
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