Key result
Binding of human spliceosomal U2 snRNP protein p14 to RNA is nonspecific and does not recognize the branch site, suggesting it screens charges on the backbone during spliceosome assembly.
The binding of p14 to RNA is nonspecific and does not recognize the branch site, suggesting it screens charges on the backbone of the branch site during spliceosome assembly.
Challenges branch site specificity models for p14; leaves open its charge-screening role in spliceosome assembly.
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.
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Perea et al. (2016) studied this question. RNA duplex representing the branch site helix vs. RNA duplex without the bulged branch site residue was evaluated on Nuclear magnetic resonance cross-peaks / chemical shift changes. Binding of human spliceosomal U2 snRNP protein p14 to RNA is nonspecific and does not recognize the branch site, suggesting it screens charges on the backbone during spliceosome assembly.
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