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 Tang, Z.
Right arrow Articles by Lin, R.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tang, Z.
Right arrow Articles by Lin, R.-J.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2000, p. 816-824, Vol. 20, No. 3
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Biochemical and Genetic Conservation of Fission Yeast Dsk1 and Human SR Protein-Specific Kinase 1

Zhaohua Tang, Tiffany Kuo, Jenny Shen, and Ren-Jang Lin*

Department of Molecular Biology, Beckman Research Institute of the City of Hope, Duarte, California 91010

Received 6 August 1999/Returned for modification 28 September 1999/Accepted 25 October 1999

Arginine/serine-rich (RS) domain-containing proteins and their phosphorylation by specific protein kinases constitute control circuits to regulate pre-mRNA splicing and coordinate splicing with transcription in mammalian cells. We present here the finding that similar SR networks exist in Schizosaccharomyces pombe. We previously showed that Dsk1 protein, originally described as a mitotic regulator, displays high activity in phosphorylating S. pombe Prp2 protein (spU2AF59), a homologue of human U2AF65. We now demonstrate that Dsk1 also phosphorylates two recently identified fission yeast proteins with RS repeats, Srp1 and Srp2, in vitro. The phosphorylated proteins bear the same phosphoepitope found in mammalian SR proteins. Consistent with its substrate specificity, Dsk1 forms kinase-competent complexes with those proteins. Furthermore, dsk1+ gene determines the phenotype of prp2+ overexpression, providing in vivo evidence that Prp2 is a target for Dsk1. The dsk1-null mutant strain became severely sick with the additional deletion of a related kinase gene. Significantly, human SR protein-specific kinase 1 (SRPK1) complements the growth defect of the double-deletion mutant. In conjunction with the resemblance of dsk1+ and SRPK1 in sequence homology, biochemical properties, and overexpression phenotypes, the complementation result indicates that SRPK1 is a functional homologue of Dsk1. Collectively, our studies illustrate the conserved SR networks in S. pombe consisting of RS domain-containing proteins and SR protein-specific kinases and thus establish the importance of the networks in eucaryotic organisms.

* Corresponding author. Mailing address: Department of Molecular Biology, Beckman Research Institute of the City of Hope, 1450 E. Duarte Rd., Duarte, CA 91010. Phone: (626) 301-8286. Fax: (626) 301-8280. E-mail: rlin{at}coh.org.

Molecular and Cellular Biology, February 2000, p. 816-824, Vol. 20, No. 3
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Liu, S., Kang, K., Zhang, J., Ouyang, Q., Zhou, Z., Tian, S., Xing, M. (2009). A novel Physarum polycephalum SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2. Acta Biochim Biophys Sin 41: 657-667 [Abstract] [Full Text]  
  • Ding, J.-H., Zhong, X.-Y., Hagopian, J. C., Cruz, M. M., Ghosh, G., Feramisco, J., Adams, J. A., Fu, X.-D. (2006). Regulated Cellular Partitioning of SR Protein-specific Kinases in Mammalian Cells. Mol. Biol. Cell 17: 876-885 [Abstract] [Full Text]  
  • Liang, X.-h., Haritan, A., Uliel, S., Michaeli, S. (2003). trans and cis Splicing in Trypanosomatids: Mechanism, Factors, and Regulation. Eukaryot Cell 2: 830-840 [Full Text]  
  • Kamachi, M., Le, T. M., Kim, S. J., Geiger, M. E., Anderson, P., Utz, P. J. (2002). Human Autoimmune Sera as Molecular Probes for the Identification of an Autoantigen Kinase Signaling Pathway. JEM 196: 1213-1226 [Abstract] [Full Text]  
  • Kaufer, N. F., Potashkin, J. (2000). SURVEY AND SUMMARY: Analysis of the splicing machinery in fission yeast: a comparison with budding yeast and mammals. Nucleic Acids Res 28: 3003-3010 [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»