The SRm160/300 splicing coactivator subunits

Benjamin J. Blencowe(University of Toronto), Göran Baurén(Center for Cancer Research), Adam G. Eldridge(Center for Cancer Research), Robbyn Issner(Idera Pharmaceuticals (United States)), Jeffrey A. Nickerson(University of Massachusetts Chan Medical School), Emanuel Rosonina(University of Toronto), Phillip A. Sharp(Center for Cancer Research)
RNA
January 1, 2000
10.1017/s1355838200991982
Cited by 127Open Access
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Abstract

The SRm160/300 splicing coactivator, which consists of the serine/arginine (SR)-related nuclear matrix protein of 160 kDa and a 300-kDa nuclear matrix antigen, functions in splicing by promoting critical interactions between splicing factors bound to pre-mRNA, including snRNPs and SR family proteins. In this article we report the isolation of a cDNA encoding the 300-kDa antigen and investigate the activity of it and SRm160 in splicing. Like SRm160, the 300-kDa antigen contains domains rich in alternating S and R residues but lacks an RNA recognition motif; the protein is accordingly named "SRm300." SRm300 also contains a novel and highly conserved N-terminal domain, several unique repeated motifs rich in S, R, and proline residues, and two very long polyserine tracts. Surprisingly, specific depletion of SRm300 does not prevent the splicing of pre-mRNAs shown previously to require SRm160/300. Addition of recombinant SRm160 alone to SRm160/300-depleted reactions specifically activates splicing. The results indicate that SRm160 may be the more critical component of the SRm160/300 coactivator in the splicing of SRm160/300-dependent pre-mRNAs.

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