| pubmed-article:8202378 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C0142661 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1424922 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:8202378 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8202378 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8202378 | pubmed:dateCreated | 1994-7-1 | lld:pubmed |
| pubmed-article:8202378 | pubmed:abstractText | The PRP4 protein of Saccharomyces cerevisiae is an essential part of the U4/U6 snRNP, a component of the mRNA splicing apparatus. As an approach to the determination of structure-function relationships in the PRP4 protein, we have isolated more than fifty new alleles of the PRP4 gene through random and site-directed mutagenesis, and have analyzed the phenotypes of many of them. Twelve of the fourteen single-point mutations that give rise to temperature-sensitive (ts) or null phenotypes are located in the portion of the PRP4 gene that corresponds to the beta-transducin-like region of the protein; the remaining two are located in the central portion of the gene, one of them in an arginine-lysine-rich region. Nine additional deletion or deletion/insertion mutations were isolated at both the amino- and carboxy-termini. These data show that the amino-terminal region (108 amino acids) of PRP4 is non-essential, while the carboxy-terminal region is essential up to the penultimate amino acid. A deletion of one entire beta-transducin-like repeat (the third of five) resulted in a null phenotype. All ts mutants show a first-step defect in the splicing of U3 snRNA primary transcript in vivo at the non-permissive temperature. The effects on prp4 mutant growth of increased copy-number of mutant prp4 genes themselves, and of genes for other components of the U4/U6 snRNP (PRP3 and U6 snRNA) have also been studied. We suggest that the PRP4 protein has at least three domains: a non-essential amino-terminal segment of at least 108 amino acids, a central basic region of about 140 residues that is relatively refractile to mutation and might be involved in RNA interaction, and an essential carboxy-terminal region of about 210 residues with the five repeat-regions that are similar to beta-transducins, which might be involved in protein-protein interaction. A model of interactions of snRNP components suggested by these results is presented. | lld:pubmed |
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| pubmed-article:8202378 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8202378 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8202378 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8202378 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8202378 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8202378 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8202378 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8202378 | pubmed:month | May | lld:pubmed |
| pubmed-article:8202378 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:WandBB | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:FriesenJ DJD | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:XuYY | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:SchappertKK | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:HuJJ | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:HarringtonTT | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:MogridgeJJ | lld:pubmed |
| pubmed-article:8202378 | pubmed:author | pubmed-author:BragaRR | lld:pubmed |
| pubmed-article:8202378 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8202378 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:8202378 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:8202378 | pubmed:geneSymbol | PRP4 | lld:pubmed |
| pubmed-article:8202378 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8202378 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8202378 | pubmed:pagination | 1724-34 | lld:pubmed |
| pubmed-article:8202378 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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