This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cazalla, D.
Right arrow Articles by Cáceres, J. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cazalla, D.
Right arrow Articles by Cáceres, J. F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2005, p. 2969-2980, Vol. 25, No. 8
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.8.2969-2980.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Novel SR-Related Protein Is Required for the Second Step of Pre-mRNA Splicing

Demian Cazalla, Kathryn Newton,{dagger} and Javier F. Cáceres*

MRC Human Genetics Unit, Edinburgh, Scotland, United Kingdom

Received 15 November 2004/ Returned for modification 15 December 2004/ Accepted 10 January 2005

The SR family proteins and SR-related polypeptides are important regulators of pre-mRNA splicing. A novel SR-related protein of an apparent molecular mass of 53 kDa was isolated in a gene trap screen that identifies proteins which localize to the nuclear speckles. This novel protein possesses an arginine- and serine-rich domain and was termed SRrp53 (for SR-related protein of 53 kDa). In support for a role of this novel RS-containing protein in pre-mRNA splicing, we identified the mouse ortholog of the Saccharomyces cerevisiae U1 snRNP-specific protein Luc7p and the U2AF65-related factor HCC1 as interacting proteins. In addition, SRrp53 is able to interact with some members of the SR family of proteins and with U2AF35 in a yeast two-hybrid system and in cell extracts. We show that in HeLa nuclear extracts immunodepleted of SRrp53, the second step of pre-mRNA splicing is blocked, and recombinant SRrp53 is able to restore splicing activity. SRrp53 also regulates alternative splicing in a concentration-dependent manner. Taken together, these results suggest that SRrp53 is a novel SR-related protein that has a role both in constitutive and in alternative splicing.

* Corresponding author. Mailing address: MRC Human Genetics Unit, Western General Hospital, Crewe Rd., Edinburgh EH4 2XU, Scotland, United Kingdom. Phone: 44 131 467 8426. Fax: 44 131 467 8456. E-mail: Javier.Caceres{at}hgu.mrc.ac.uk.

{dagger} Present address: Virginia Mason Research Center, Seattle, WA 98101.

Molecular and Cellular Biology, April 2005, p. 2969-2980, Vol. 25, No. 8
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.8.2969-2980.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Laserna, E. J., Valero, M. L., Sanz, L., Sanchez del Pino, M. M., Calvete, J. J., Barettino, D. (2009). Proteomic Analysis of Phosphorylated Nuclear Proteins Underscores Novel Roles for Rapid Actions of Retinoic Acid in the Regulation of mRNA Splicing and Translation. Mol. Endocrinol. 23: 1799-1814 [Abstract] [Full Text]  
  • Grillari, J., Loscher, M., Denegri, M., Lee, K., Fortschegger, K., Eisenhaber, F., Ajuh, P., Lamond, A. I., Katinger, H., Grillari-Voglauer, R. (2009). Blom7{alpha} Is a Novel Heterogeneous Nuclear Ribonucleoprotein K Homology Domain Protein Involved in Pre-mRNA Splicing That Interacts with SNEVPrp19-Pso4. J. Biol. Chem. 284: 29193-29204 [Abstract] [Full Text]  
  • Ellis, J. D., Lleres, D., Denegri, M., Lamond, A. I., Caceres, J. F. (2008). Spatial mapping of splicing factor complexes involved in exon and intron definition. JCB 181: 921-934 [Abstract] [Full Text]  
  • Zhou, A., Ou, A. C., Cho, A., Benz, E. J. Jr., Huang, S.-C. (2008). Novel Splicing Factor RBM25 Modulates Bcl-x Pre-mRNA 5' Splice Site Selection. Mol. Cell. Biol. 28: 5924-5936 [Abstract] [Full Text]  
  • Howell, V. M., Jones, J. M., Bergren, S. K., Li, L., Billi, A. C., Avenarius, M. R., Meisler, M. H. (2007). Evidence for a direct role of the disease modifier SCNM1 in splicing. Hum Mol Genet 16: 2506-2516 [Abstract] [Full Text]  
  • Puig, O., Bragado-Nilsson, E., Koski, T., Seraphin, B. (2007). The U1 snRNP-associated factor Luc7p affects 5' splice site selection in yeast and human. Nucleic Acids Res 35: 5874-5885 [Abstract] [Full Text]  
  • Tillemans, V., Leponce, I., Rausin, G., Dispa, L., Motte, P. (2006). Insights into Nuclear Organization in Plants as Revealed by the Dynamic Distribution of Arabidopsis SR Splicing Factors. Plant Cell 18: 3218-3234 [Abstract] [Full Text]  
  • Mangs, A. H., Speirs, H. J.L., Goy, C., Adams, D. J., Markus, M. A., Morris, B. J. (2006). XE7: A novel splicing factor that interacts with ASF/SF2 and ZNF265. Nucleic Acids Res 34: 4976-4986 [Abstract] [Full Text]  
  • Vanhoutteghem, A., Djian, P. (2006). Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions. Proc. Natl. Acad. Sci. USA 103: 12423-12428 [Abstract] [Full Text]  
  • Guil, S., Long, J. C., Caceres, J. F. (2006). hnRNP A1 Relocalization to the Stress Granules Reflects a Role in the Stress Response. Mol. Cell. Biol. 26: 5744-5758 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»