General splicing factor SF2/ASF promotes alternative splicing by binding to an exonic splicing enhancer.
The general splicing factor SF2/ASF binds in a sequence-specific manner to a purine-rich exonic splicing enhancer (ESE) in the last exon of bovine growth hormone (bGH) pre-mRNA. More importantly, SF2/ASF stimulates in vitro splicing of bGH intron D through specific interaction with the ESE sequences. However, another general splicing factor, SC35, does not bind the ESE sequences and has no effect on bGH intron D splicing. Thus, one possible function of SF2/ASF in alternative and, perhaps, constitutive pre-mRNA splicing is to recognize ESE sequences. The stimulation of bGH intron D splicing by SF2/ASF is counteracted by the addition of hnRNP A1. The relative levels of SF2/ASF and hnRNP A1 influence the efficiency of bGH intron D splicing in vitro and may be the underlying mechanism of this alternative pre-mRNA processing event in vivo.
Sun
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Department of Molecular Biology and Microbiology, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106-4960.
Mayeda
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A
Hampson
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RK
Krainer
A R
AR
Rottman
F M
FM
D017398:Alternative Splicing / Q000502:physiology*; D000818:Animals; D002417:Cattle; D004742:Enhancer Elements, Genetic / Q000502:physiology*; D013006:Growth Hormone / Q000235:genetics*; D006367:HeLa Cells; D006801:Humans; D009687:Nuclear Proteins / Q000378:metabolism / Q000502:physiology*; D012332:RNA, Heterogeneous Nuclear / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism / Q000502:physiology*; D000068103:Serine-Arginine Splicing Factors
D009687:Nuclear Proteins; D012332:RNA, Heterogeneous Nuclear; D016601:RNA-Binding Proteins; D000068103:Serine-Arginine Splicing Factors; D013006:Growth Hormone