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Nucleic Acids Research Advance Access originally published online on May 30, 2007
Nucleic Acids Research 2007 35(12):3928-3944; doi:10.1093/nar/gkm347
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Nucleic Acids Research, 2007, Vol. 35, No. 12 3928-3944
© 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.

RNA

Proteomic analysis of in vivo-assembled pre-mRNA splicing complexes expands the catalog of participating factors

Yen-I G. Chen1, Roger E. Moore2, Helen Y. Ge2, Mary K. Young2, Terry D. Lee2 and Scott W. Stevens1,3,4,*

1Graduate program in Microbiology, 2City of Hope Beckman Research Institute, Duarte, CA 91010, 3Section of Molecular Genetics and Microbiology, University of Texas at Austin, 1 University, Station #A4800, Austin, TX 78712 and 4Institute for Cellular and Molecular Biology, University of Texas at Austin, TX, USA

*To whom correspondence should be addressed. Tel: +1-512-232-9303; Fax: +1-512-232-3432; Email: scott.stevens{at}mail.utexas.edu

Received March 14, 2007. Revised April 19, 2007. Accepted April 20, 2007.

Previous compositional studies of pre-mRNA processing complexes have been performed in vitro on synthetic pre-mRNAs containing a single intron. To provide a more comprehensive list of polypeptides associated with the pre-mRNA splicing apparatus, we have determined the composition of the bulk pre-mRNA processing machinery in living cells. We purified endogenous nuclear pre-mRNA processing complexes from human and chicken cells comprising the massive (>200S) supraspliceosomes (a.k.a. polyspliceosomes). As expected, RNA components include a heterogeneous mixture of pre-mRNAs and the five spliceosomal snRNAs. In addition to known pre-mRNA splicing factors, 5' end binding factors, 3' end processing factors, mRNA export factors, hnRNPs and other RNA binding proteins, the protein components identified by mass spectrometry include RNA adenosine deaminases and several novel factors. Intriguingly, our purified supraspliceosomes also contain a number of structural proteins, nucleoporins, chromatin remodeling factors and several novel proteins that were absent from splicing complexes assembled in vitro. These in vivo analyses bring the total number of factors associated with pre-mRNA to well over 300, and represent the most comprehensive analysis of the pre-mRNA processing machinery to date.


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