Abstract
We have probed the molecular basis of recognition between human spliceosomal U2 snRNP protein p14 and RNA targets representing the intron branch site region. Interaction of an RNA duplex representing the branch site helix perturbed at least 10 nuclear magnetic resonance cross-peaks of (15)N-labeled p14. However, similar chemical shift changes were observed upon interaction with a duplex without the bulged branch site residue, suggesting that binding of p14 to RNA is nonspecific and does not recognize the branch site. We propose that the p14-RNA interaction screens charges on the backbone of the branch site during spliceosome assembly.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Humans
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RNA Precursors / chemistry*
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RNA Precursors / genetics
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RNA Precursors / metabolism
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RNA, Double-Stranded / chemistry*
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RNA, Double-Stranded / genetics
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RNA, Double-Stranded / metabolism
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RNA-Binding Proteins / chemistry*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism
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Ribonucleoprotein, U2 Small Nuclear / chemistry*
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Ribonucleoprotein, U2 Small Nuclear / genetics
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Ribonucleoprotein, U2 Small Nuclear / metabolism
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Spliceosomes / chemistry*
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Spliceosomes / genetics
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Spliceosomes / metabolism
Substances
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RNA Precursors
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RNA, Double-Stranded
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RNA-Binding Proteins
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Ribonucleoprotein, U2 Small Nuclear