Nucleic Acids Research Advance Access originally published online on August 28, 2007
Nucleic Acids Research 2007 35(17):5874-5885; doi:10.1093/nar/gkm505
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Nucleic Acids Research, 2007, Vol. 35, No. 17 5874-5885
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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The U1 snRNP-associated factor Luc7p affects 5' splice site selection in yeast and human
1European Molecular Biology Laboratory, Meyerhofstrasse, 1, 69117 Heidelberg, Germany, 2Institute of Biotechnology, University of Helsinki, Viikinkaari 9, 00014 Helsinki, Finland and 3CGM, CNRS, Avenue de la Terrasse, 91198 Gif sur Yvette Cedex, France
*To whom correspondence should be addressed. Tel: +358 9191 59423; Fax: +358 9191 59366; Email: oscar.puig{at}helsinki.fi Correspondence may also be addressed to Bertrand Séraphin. Tel: +33 1 69 82 38 84; Fax: +33 1 69 82 38 77; Email: seraphin{at}cgm.cnrs-gif.fr
Received March 16, 2007. Revised June 10, 2007. Accepted June 11, 2007.
yLuc7p is an essential subunit of the yeast U1 snRNP and contains two putative zinc fingers. Using RNA–protein cross-linking and directed site-specific proteolysis (DSSP), we have established that the N-terminal zinc finger of yLuc7p contacts the pre-mRNA in the 5' exon in a region close to the cap. Modifying the pre-mRNA sequence in the region contacted by yLuc7p affects splicing in a yLuc7p-dependent manner indicating that yLuc7p stabilizes U1 snRNP–pre-mRNA interaction, thus reminding of the mode of action of another U1 snRNP component, Nam8p. Database searches identified three putative human yLuc7p homologs (hLuc7A, hLuc7B1 and hLuc7B2). These proteins have an extended C-terminal tail rich in RS and RE residues, a feature characteristic of splicing factors. Consistent with a role in pre-mRNA splicing, hLuc7A localizes in the nucleus and antibodies raised against hLuc7A specifically co-precipitate U1 snRNA from human cell extracts. Interestingly, hLuc7A overexpression affects splicing of a reporter in vivo. Taken together, our data suggest that the formation of a wide network of protein–RNA interactions around the 5' splice site by U1 snRNP-associated factors contributes to alternative splicing regulation.
Present address: Elisabeth Bragado-Nilsson, Centro Nacional de Investigaciones Oncológicas, Melchor Fernàndez Almagro, 3, E-28029 Madrid, Spain
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