Analysis of interacting partners and alternative splicing isoforms of human Splicing Factor 1

Diplôme Thèse Analysis of interacting partners and alternative splicing isoforms of human Splicing Factor 1 eng 2014-12-17 author Crisci Angela 702657 director Kraemer Angela 22808 10.13097/archive-ouverte/unige:45687 urn:nbn:ch:unige-456879 Sc. 4748 During the splicing reaction, introns are removed from the pre-mRNA and exons are joined together. This process occurs in a stepwise manner and is carried out by the spliceosome, which consists of five snRNPs and hundreds of proteins. Splicing Factor 1 (SF1) acts at the onset of spliceosome assembly by recognizing the intron branch-point sequence (BPS) in the early complex E. SF1 is then displaced from the pre-mRNA and the BPS is recognized by U2 snRNP in complex A. In this study, we identified novel SF1-interacting partners by performing yeast-two-hybrid screens and co-immunoprecipitation coupled to mass spectrometry. Our results show that SF1 interacts both in vitro and in HeLa nuclear extracts with SURP domains of the U2 snRNP-associated proteins SF3a120 and CHERP. This interaction is required for efficient formation of complex A by promoting the association of U2 snRNP with the spliceosome. Splicing Factor 1 Spliceosome U2 snRNP SURP domains CHERP Dewey 570 46 Département de biologie cellulaire 165 false 75083fcb-b5e7-4ce5-a397-8f2560da9f9d Thesis Public Thesis-Crisci.pdf 15220758 application/pdf Private 2015-07-13 bfc211324cb00e7771d8996b8cf488abfec4d0e3f01771db3d9a69a6e04238b1 openAccess Faculté des sciences / Section de biologie / Département de biologie cellulaire

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Analysis of interacting partners and alternative splicing isoforms of human Splicing Factor 1				2014	970	318

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Crisci, Angela