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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#_5 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#_4 http://www.w3.org/ns/prov#value The splicing of the c-src exon N1 is controlled by an intricate combination of positive and negative RNA elements. Most previous work on these sequences focused on intronic elements found upstream and downstream of exon N1. However, it was demonstrated that the 5' half of the N1 exon itself acts as a splicing enhancer in vivo. Here we examine the function of this regulatory element in vitro. We show that a mutation in this sequence decreases splicing of the N1 exon in vitro. Proteins binding to this element were identified as hnRNP A1, hnRNP H, hnRNP F, and SF2/ASF by site-specific cross-linking and immunoprecipitation. The binding of these proteins to the RNA was eliminated by a mutation in the exonic element. The activities of hnRNP A1 and SF2/ASF on N1 splicing were examined by adding purified protein to in vitro splicing reactions. SF2/ASF and another SR protein, SC35, are both able to stimulate splicing of c-src pre-mRNA. However, splicing activation by SF2/ASF is dependent on the N1 exon enhancer element whereas activation by SC35 is not. In contrast to SF2/ASF and in agreement with other systems, hnRNP A1 repressed c-src splicing in vitro. The negative activity of hnRNP A1 on splicing was compared with that of PTB, a protein previously demonstrated to repress splicing in this system. Both proteins repress exon N1 splicing, and both counteract the enhancing activity of the SR proteins. Removal of the PTB binding sites upstream of N1 prevents PTB-mediated repression but does not affect A1-mediated repression. Thus, hnRNP A1 and PTB use different mechanisms to repress c-src splicing. Our results link the activity of these well-known exonic splicing regulators, SF2/ASF and hnRNP A1, to the splicing of an exon primarily controlled by intronic factors. In contrast to SF2/ASF and in agreement with other systems, hnRNP A1 repressed c-src splicing in vitro. http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#_4 http://www.w3.org/ns/prov#wasQuotedFrom http://www.ncbi.nlm.nih.gov/pubmed/12612063 http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#_5 http://www.w3.org/2000/01/rdf-schema#label Selventa http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#assertion http://www.w3.org/ns/prov#hadPrimarySource http://www.ncbi.nlm.nih.gov/pubmed/12612063 http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#_4 http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA#pubinfo http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA http://purl.org/dc/terms/created 2014-07-03T14:30:10.633+02:00 http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA http://purl.org/pav/createdBy http://orcid.org/0000-0001-6818-334X http://www.tkuhn.ch/bel2nanopub/RACmHigHyIuC7So0vtTXiAY5gybNUCcLvC1hEQGgqKmYA http://purl.org/pav/createdBy http://orcid.org/0000-0002-1267-0234