Source:http://linkedlifedata.com/resource/pubmed/id/10923022
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2000-9-14
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pubmed:abstractText |
The prp2 gene of fission yeast has previously been shown to encode the large subunit of the splicing factor spU2AF. SpU2AF(59) is an evolutionarily conserved protein that has an arginine/serine-rich region and three RNA recognition motifs (RRMs). We have sequenced three temperature-sensitive alleles of prp2 and determined that the mutations result in single amino acid changes within one of the RRMs or between RRMs. All mutant alleles of prp2 have pre-mRNA splicing defects at the non-permissive temperature. Although the mutant strains are growth-arrested at 37 degrees C, they do not elongate like typical fission yeast cell cycle mutants. The DNA of the prp2(-) strains stains more intensely than a wild-type strain, suggesting that the chromatin may be condensed. Ultrastructural studies show differences in the mutant nuclei including a prominent distinction between the chromatin- and non-chromatin-enriched regions compared to the more homogenous wild-type nucleus. Two-hybrid assays indicate that some of the wild-type protein interactions are altered in the mutant strains. These results suggest that normal functioning of spU2AF(59) may be essential not only for pre-mRNA splicing but also for the maintenance of proper nuclear structure and normal cell cycle progression.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DEAD-box RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyurea,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRP2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/splicing factor U2AF
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0749-503X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 John Wiley & Sons, Ltd.
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1001-13
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10923022-Alleles,
pubmed-meshheading:10923022-Cell Cycle,
pubmed-meshheading:10923022-Cell Nucleus,
pubmed-meshheading:10923022-DEAD-box RNA Helicases,
pubmed-meshheading:10923022-Fungal Proteins,
pubmed-meshheading:10923022-Hydroxyurea,
pubmed-meshheading:10923022-Mutation,
pubmed-meshheading:10923022-Nuclear Proteins,
pubmed-meshheading:10923022-RNA, Fungal,
pubmed-meshheading:10923022-RNA Precursors,
pubmed-meshheading:10923022-RNA Splicing,
pubmed-meshheading:10923022-Ribonucleoproteins,
pubmed-meshheading:10923022-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10923022-Schizosaccharomyces,
pubmed-meshheading:10923022-Temperature,
pubmed-meshheading:10923022-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
Mutations in the large subunit of U2AF disrupt pre-mRNA splicing, cell cycle progression and nuclear structure.
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pubmed:affiliation |
Department of Cellular and Molecular Pharmacology, Finch University of Health Sciences/The Chicago Medical School, 3333 Green Bay Road, North Chicago, IL 60064, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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