| pubmed-article:2149118 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2149118 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:2149118 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:2149118 | lifeskim:mentions | umls-concept:C0041532 | lld:lifeskim |
| pubmed-article:2149118 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:2149118 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:2149118 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:2149118 | pubmed:issue | 12B | lld:pubmed |
| pubmed-article:2149118 | pubmed:dateCreated | 1991-3-14 | lld:pubmed |
| pubmed-article:2149118 | pubmed:abstractText | U6 is the most highly conserved of the five spliceosomal RNAs. It is associated with U4 by an extensive base-pairing interaction, which is disrupted immediately prior to the first nucleolytic step of splicing. It has been proposed that this event activates catalysis by unmasking U6. Using a combination of doped synthesis and site-directed mutagenesis to generate point mutations in U6, we have now identified 12 positions, in three domains, at which single nucleotide substitutions or deletions result in lethal or temperature-sensitive phenotypes. Biochemical analysis demonstrates that most of these mutants retain the ability to assemble into U4/U6 and U4/U5/U6 snRNPs. Notably, although mutations at three positions in U6 that base-pair with U4 are lethal, mutations in the complementary residues in U4 are fully viable. Furthermore, compensatory mutations in U4 that restore base-pairing fail to suppress the phenotypes of the U6 mutations. This demonstrates a function for U6 independent of its role in base-pairing. Remarkably, two of the three essential regions in U6 identified genetically correspond to intron insertion points in two yeast species. A temperature-sensitive mutation at one of these sites is defective in the second step of splicing in vitro. | lld:pubmed |
| pubmed-article:2149118 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2149118 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2149118 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2149118 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2149118 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2149118 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2149118 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:2149118 | pubmed:author | pubmed-author:GuthrieCC | lld:pubmed |
| pubmed-article:2149118 | pubmed:author | pubmed-author:MadhaniH DHD | lld:pubmed |
| pubmed-article:2149118 | pubmed:author | pubmed-author:BordonnéRR | lld:pubmed |
| pubmed-article:2149118 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2149118 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:2149118 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2149118 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2149118 | pubmed:pagination | 2264-77 | lld:pubmed |
| pubmed-article:2149118 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2149118 | pubmed:meshHeading | pubmed-meshheading:2149118-... | lld:pubmed |
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| pubmed-article:2149118 | pubmed:meshHeading | pubmed-meshheading:2149118-... | lld:pubmed |
| pubmed-article:2149118 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2149118 | pubmed:articleTitle | Multiple roles for U6 snRNA in the splicing pathway. | lld:pubmed |
| pubmed-article:2149118 | pubmed:affiliation | Department of Biochemistry and Biophysics, University of California, San Francisco 94143. | lld:pubmed |
| pubmed-article:2149118 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2149118 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2149118 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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