Nucleic Acids Research Advance Access published online on September 18, 2006
Nucleic Acids Research, doi:10.1093/nar/gkl660
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© 2006 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.
Molecular Biology |
XE7: A novel splicing factor that interacts with ASF/SF2 and ZNF265
Basic & Clinical Genomics Laboratory, School of Medical Sciences and Bosch Institute, The University of Sydney NSW 2006, Australia
*To whom correspondence should be addressed. Tel: +61-2-93513688; Fax: +61-2-93512227; Email: brianm{at}medsci.usyd.edu.au
Received August 18, 2006. Revised August 18, 2006. Accepted August 28, 2006.
Pre-mRNA splicing is performed by the spliceosome. SR proteins in this macromolecular complex are essential for both constitutive and alternative splicing. By using the SR-related protein ZNF265 as bait in a yeast two-hybrid screen, we pulled out the uncharacterized human protein XE7, which is encoded by a pseudoautosomal gene. XE7 had been identified in a large-scale proteomic analysis of the human spliceosome. It consists of two different isoforms produced by alternative splicing. The arginine/serine (RS)-rich region in the larger of these suggests a role in mRNA processing. Herein we show for the first time that XE7 is an alternative splicing regulator. XE7 interacts with ZNF265, as well as with the essential SR protein ASF/SF2. The RS-rich region of XE7 dictates both interactions. We show that XE7 localizes in the nucleus of human cells, where it colocalizes with both ZNF265 and ASF/SF2, as well as with other SR proteins, in speckles. We also demonstrate that XE7 influences alternative splice site selection of pre-mRNAs from CD44, Tra2-ß1 and SRp20 minigenes. We have thus shown that the spliceosomal component XE7 resembles an SR-related splicing protein, and can influence alternative splicing.
Present addresses: Helen J.L. Speirs, Clive & Vera Ramaciotti Centre for Gene Function Analysis, School of Biotechnology & Biomolecular Sciences, University of New South Wales, Sydney NSW 2052, Australia
David J. Adams, The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambs CB10 1SA, UK
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