MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow An erratum has been published
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 Sakashita, E.
Right arrow Articles by Mayeda, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sakashita, E.
Right arrow Articles by Mayeda, A.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2004, p. 1174-1187, Vol. 24, No. 3
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.3.1174-1187.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Human RNPS1 and Its Associated Factors: a Versatile Alternative Pre-mRNA Splicing Regulator In Vivo

Eiji Sakashita,1,2 Sawako Tatsumi,1,{dagger} Dieter Werner,3 Hitoshi Endo,2 and Akila Mayeda1*

Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33136-1019,1 Department of Biochemistry, Jichi Medical School, Tochigi 329-0498, Japan,2 Division of Biochemistry of the Cell, German Cancer Research Center, Heidelberg D-69120, Germany3

Received 27 June 2003/ Returned for modification 12 August 2003/ Accepted 29 October 2003

Human RNPS1 was originally purified and characterized as a pre-mRNA splicing activator, and its role in the postsplicing process has also been proposed recently. To search for factors that functionally interact with RNPS1, we performed a yeast two-hybrid screen with a human cDNA library. Four factors were identified: p54 (also called SRp54; a member of the SR protein family), human transformer 2ß (hTra2ß; an exonic splicing enhancer-binding protein), hLucA (a potential component of U1 snRNP), and pinin (also called DRS and MemA; a protein localized in nuclear speckles). The N-terminal region containing the serine-rich (S) domain, the central RNA recognition motif (RRM), and the C-terminal arginine/serine/proline-rich (RS/P) domain of RNPS1 interact with p54, pinin, and hTra2ß, respectively. Protein-protein binding between RNPS1 and these factors was verified in vitro and in vivo. Overexpression of RNPS1 in HeLa cells induced exon skipping in a model ß-globin pre-mRNA and a human tra-2ß pre-mRNA. Coexpression of RNPS1 with p54 cooperatively stimulated exon inclusion in an ATP synthase {gamma}-subunit pre-mRNA. The RS/P domain and RRM are necessary for the exon-skipping activity, whereas the S domain is important for the cooperative effect with p54. RNPS1 appears to be a versatile factor that regulates alternative splicing of a variety of pre-mRNAs.


* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, P.O. Box 016129, Miami, FL 33101-6129. Phone: (305) 243-4621. Fax: (305) 243-3065. E-mail: mayeda{at}miami.edu.

{dagger} Present address: Department of Geriatric Research, National Institute for Longevity Sciences, Aichi 474-8522, Japan.


Molecular and Cellular Biology, February 2004, p. 1174-1187, Vol. 24, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.3.1174-1187.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2004 by the American Society for Microbiology. All rights reserved.