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• W268783301 abstract "Research Article1 December 1993free access Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains. J.F. Cáceres J.F. Cáceres Cold Spring Harbor Laboratory, NY 11724-2208. Search for more papers by this author A.R. Krainer A.R. Krainer Cold Spring Harbor Laboratory, NY 11724-2208. Search for more papers by this author J.F. Cáceres J.F. Cáceres Cold Spring Harbor Laboratory, NY 11724-2208. Search for more papers by this author A.R. Krainer A.R. Krainer Cold Spring Harbor Laboratory, NY 11724-2208. Search for more papers by this author Author Information J.F. Cáceres1 and A.R. Krainer1 1Cold Spring Harbor Laboratory, NY 11724-2208. The EMBO Journal (1993)12:4715-4726https://doi.org/10.1002/j.1460-2075.1993.tb06160.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Human pre-mRNA splicing factor SF2/ASF has an activity required for general splicing in vitro and promotes utilization of proximal alternative 5′ splice sites in a concentration-dependent manner by opposing hnRNP A1. We introduced selected mutations in the N-terminal RNA recognition motif (RRM) and the C-terminal Arg/Ser (RS) domain of SF2/ASF, and assayed the resulting recombinant proteins for constitutive and alternative splicing in vitro and for binding to pre-mRNA and mRNA. Mutants inactive in constitutive splicing can affect alternative splice site selection, demonstrating that these activities involve distinct molecular interactions. Specific protein-RNA contact mediated by Phe56 and Phe58 in the RNP-1 submotif of the SF2/ASF RRM are essential for constitutive splicing, although they are not required for RRM-mediated binding to pre-mRNA. The RS domain is also required for constitutive splicing activity and both Arg and Ser residues are important. Analysis of domain deletion mutants demonstrated strong synergy between the RRM and a central degenerate RRM repeat in binding to RNA. These two domains are sufficient for alternative splicing activity in the absence of an RS domain. Previous ArticleNext Article Volume 12Issue 121 December 1993In this issue RelatedDetailsLoading ..." @default.
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• W268783301 date "1993-12-01" @default.
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• W268783301 title "Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains." @default.
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• W268783301 doi "https://doi.org/10.1002/j.1460-2075.1993.tb06160.x" @default.
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