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Protein–protein interactions and 5'-splice-site recognition in mammalian mRNA precursors

Nature volume 368, pages 119–124 (1994)Cite this article

Abstract

Exactly how specific splice sites are recognized during the processing of complex precursor messenger RNAs is not clear. Small nuclear ribonucleoprotein particles (snRNPs) are involved, but are not sufficient by themselves to define splice sites. Now a human protein essential for splicing in vitro, called alternative splicing factor/splicing factor 2, is shown to cooperate with the U1 snRNP particle in binding pre-mRNA. This cooperation is probably achieved by specific interactions between the arginine/serine-rich domain of the splicing factor and a similar region in a U1 snRNP-specific protein.

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Author notes

  1. Ping Zuo

    Present address: Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts, 02138, USA

Authors and Affiliations

  1. Department of Biological Sciences, Columbia University, New York, New York, 10027, USA

    Jhumku D. Kohtz, Ping Zuo & James L. Manley

  2. Department of Molecular Cancer Biology, Department of Microbiology, Department of Medicine, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Sharon F. Jamison & Mariano A. Garcia-Blanco

  3. Institut für Molekularbiologie und Tumorforschung, Philipps-Universität, Marburg, Emil-Mannkopff-Strasse 2, D-35037, Marburg, Germany

    Cindy L. Will & Reinhard Lührmann

Authors
  1. Jhumku D. Kohtz
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  2. Sharon F. Jamison
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  3. Cindy L. Will
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  4. Ping Zuo
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  5. Reinhard Lührmann
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  6. Mariano A. Garcia-Blanco
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  7. James L. Manley
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Kohtz, J., Jamison, S., Will, C. et al. Protein–protein interactions and 5'-splice-site recognition in mammalian mRNA precursors. Nature 368, 119–124 (1994). https://doi.org/10.1038/368119a0

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