| pubmed-article:17320109 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17320109 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:17320109 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:17320109 | lifeskim:mentions | umls-concept:C1522002 | lld:lifeskim |
| pubmed-article:17320109 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:17320109 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17320109 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:17320109 | pubmed:dateCreated | 2007-3-20 | lld:pubmed |
| pubmed-article:17320109 | pubmed:abstractText | The essential Saccharomyces cerevisiae pre-messenger RNA splicing protein 24 (Prp24) has four RNA recognition motifs (RRMs) and facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 is a component of the free U6 small nuclear ribonucleoprotein particle (snRNP) but not the U4/U6 bi-snRNP, and so is thought to be displaced from U6 by U4/U6 base-pairing. The interaction partners of each of the four RRMs of Prp24 and how these interactions direct U4/U6 pairing are not known. Here we report the crystal structure of the first three RRMs and the solution structure of the first two RRMs of Prp24. Strikingly, RRM 2 forms extensive inter-domain contacts with RRMs 1 and 3. These contacts occupy much of the canonical RNA-binding faces (beta-sheets) of RRMs 1 and 2, but leave the beta-sheet of RRM 3 exposed. Previously identified substitutions in Prp24 that suppress mutations in U4 and U6 spliceosomal RNAs cluster primarily in the beta-sheet of RRM 3, but also in a conserved loop of RRM 2. RNA binding assays and chemical shift mapping indicate that a large basic patch evident on the surface of RRMs 1 and 2 is part of a high affinity U6 RNA binding site. Our results suggest that Prp24 binds free U6 RNA primarily with RRMs 1 and 2, which may remodel the U6 secondary structure. The beta-sheet of RRM 3 then influences U4/U6 pairing through interaction with an unidentified ligand. | lld:pubmed |
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| pubmed-article:17320109 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17320109 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17320109 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17320109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17320109 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17320109 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17320109 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:ReiterNichola... | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:PhillipsGeorg... | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:BrowDavid ADA | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:ButcherSamuel... | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:LeeDonghanD | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:BaeEuiyoungE | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:BingmanCraig... | lld:pubmed |
| pubmed-article:17320109 | pubmed:author | pubmed-author:KwanSharon... | lld:pubmed |
| pubmed-article:17320109 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17320109 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:17320109 | pubmed:volume | 367 | lld:pubmed |
| pubmed-article:17320109 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17320109 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17320109 | pubmed:pagination | 1447-58 | lld:pubmed |
