Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA.

@article{Nottrott1999FunctionalIO,
  title={Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA.},
  author={Stephanie Nottrott and Klaus Hartmuth and Patrizia Fabrizio and Henning Urlaub and I Vidovi{\'c} and Ralf Ficner and Reinhard L{\"u}hrmann},
  journal={The EMBO journal},
  year={1999},
  volume={18 21},
  pages={6119-33}
}
Activation of the spliceosome for splicing catalysis requires the dissociation of U4 snRNA from the U4/U6 snRNA duplex prior to the first step of splicing. We characterize an evolutionarily conserved 15.5 kDa protein of the HeLa [U4/U6.U5] tri-snRNP that binds directly to the 5' stem-loop of U4 snRNA. This protein shares a novel RNA recognition motif with several RNP-associated proteins, which is essential, but not sufficient for RNA binding. The 15.5kD protein binding site on the U4 snRNA… CONTINUE READING
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snRNP structure and function

  • C. L. Will, R. Lührmann
  • Eukaryotic mRNA Processing
  • 1997
Highly Influential
2 Excerpts

Splicing of precursors to mRNA by the spliceosome

  • M. J. Moore, C. C. Query, P. A. Sharp
  • The RNA World. Cold Spring Harbor Laboratory…
  • 1993
Highly Influential
3 Excerpts

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