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| Cell May (1997); 89(3):403-12 | |
| Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. | |
| Abovich N, Rosbash M | |
| Howard Hughes Medical Institute, Department of Biology, Brandeis University, Waltham, Massachusetts 02254, USA. | |
| Abstract: The commitment complex is the first defined step in the yeast (S. cerevisiae) splicing pathway. It contains U1 snRNP as well as Mud2p, which resembles human U2AF65. In a genetic screen, we identified the yeast gene MSL-5, which is a novel commitment complex component. Genetic and biochemical criteria indicate a direct interaction between Msl5p and both Mud2p and the U1 snRNP protein Prp40p. This defines a bridge between the two ends of the intron. Msl5p (renamed BBP for branchpoint bridging protein) has a mammalian ortholog, the splicing factor SF1. Our results show that SF1 interacts strongly with human U2AF65, and that SF1 is a bona fide E complex component. This implies that aspects of these novel cross-intron protein-protein interactions are conserved between yeast and mammals. | |
| [PUBMED: 9150140] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |