rdf:type |
|
lifeskim:mentions |
umls-concept:C0030685,
umls-concept:C0073438,
umls-concept:C0162771,
umls-concept:C0205224,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1413955,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1963578
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pubmed:issue |
20
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pubmed:dateCreated |
2002-5-13
|
pubmed:abstractText |
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 ((119)GSGKT(123)), II ((215)DEAH(218)) and VI ((423)QRAGRAGR(430)) 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.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/PRP43 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/lariat debranching enzyme
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17743-50
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11886864-Adenosine Triphosphatases,
pubmed-meshheading:11886864-Adenosine Triphosphate,
pubmed-meshheading:11886864-DEAD-box RNA Helicases,
pubmed-meshheading:11886864-DNA Mutational Analysis,
pubmed-meshheading:11886864-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11886864-Introns,
pubmed-meshheading:11886864-Mutagenesis, Site-Directed,
pubmed-meshheading:11886864-Phenotype,
pubmed-meshheading:11886864-RNA, Fungal,
pubmed-meshheading:11886864-RNA Helicases,
pubmed-meshheading:11886864-RNA Nucleotidyltransferases,
pubmed-meshheading:11886864-Saccharomyces cerevisiae,
pubmed-meshheading:11886864-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11886864-Spliceosomes
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pubmed:year |
2002
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pubmed:articleTitle |
Prp43 is an essential RNA-dependent ATPase required for release of lariat-intron from the spliceosome.
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pubmed:affiliation |
Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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