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  • The EMBO Journal (1999) 18, 4560 - 4570
  • doi:10.1093/emboj/18.16.4560

Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing

Akila Mayeda1, Joseph Badolato2,3, Ryuji Kobayashi4, Michael Q. Zhang4, Edith M. Gardiner2 and Adrian R. Krainer4

  1. Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, FL 33136, USA
  2. Bone and Mineral Research Program, Garvan Institute of Medical Research, Sydney, NSW 2010, Australia
  3. Present address: Eli Lilly Australia, Pty. Ltd, West Ryde, NSW 2114, Australia
  4. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA

Correspondence to:

Akila Mayeda, E-mail: amayeda@molbio.med.miami.edu

Received 12 April 1999; Accepted 2 July 1999; Revised 2 July 1999

Biochemical purification of a pre-mRNA splicing activity from HeLa cells that stimulates distal alternative 3' splice sites in a concentration-dependent manner resulted in the identification of RNPS1, a novel general activator of pre-mRNA splicing. RNPS1 cDNAs, encoding a putative nucleic-acid-binding protein of unknown function, were previously identified in mouse and human. RNPS1 is conserved in metazoans and has an RNA-recognition motif preceded by an extensive serine-rich domain. Recombinant human RNPS1 expressed in baculovirus functionally synergizes with SR proteins and strongly activates splicing of both constitutively and alternatively spliced pre-mRNAs. We conclude that RNPS1 is not only a potential regulator of alternative splicing but may also play a more fundamental role as a general activator of pre-mRNA splicing.

  • Keywords:

    • alternative splicing,
    • RNA-recognition motif,
    • RNPS1,
    • splicing activator,
    • splicing factor