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• W979014048 abstract "Research Article1 October 1992free access Roles of PRP8 protein in the assembly of splicing complexes. J.D. Brown J.D. Brown Institute of Cell and Molecular Biology, University of Edinburgh, UK. Search for more papers by this author J.D. Beggs J.D. Beggs Institute of Cell and Molecular Biology, University of Edinburgh, UK. Search for more papers by this author J.D. Brown J.D. Brown Institute of Cell and Molecular Biology, University of Edinburgh, UK. Search for more papers by this author J.D. Beggs J.D. Beggs Institute of Cell and Molecular Biology, University of Edinburgh, UK. Search for more papers by this author Author Information J.D. Brown1 and J.D. Beggs1 1Institute of Cell and Molecular Biology, University of Edinburgh, UK. The EMBO Journal (1992)11:3721-3729https://doi.org/10.1002/j.1460-2075.1992.tb05457.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Three different approaches have been used to investigate the roles of the yeast U5 snRNP protein PRP8 in spliceosome assembly: genetic depletion of PRP8 protein in vivo, heat inactivation of temperature-sensitive prp8 protein in protoplasts and inhibition of PRP8 function with antibodies in vitro. In each case, U5 and U4/U6 snRNPs failed to assemble into the forming spliceosomes. In addition, extract prepared from PRP8-depleted cells and extract containing inactivated PRP8 protein had substantially reduced amounts of U4/U6.U5 triple snRNP complexes. Thus, functional PRP8 protein is required for the stable formation of U4/U6.U5 complexes without which spliceosomes fail to form. As spliceosome formation was also blocked by anti-PRP8 antibodies that apparently do not disrupt triple snRNPs, PRP8 protein may play a separate role in the assembly of triple snRNPs into spliceosomes. As a consequence of PRP8 depletion the levels of the U4, U5 and U6 snRNAs declined dramatically. We discuss this in the context of the known genetic interactions between PRP8 and putative RNA helicase (DEAD box protein) genes and propose that PRP8 protein plays a role in regulating dynamic RNA-RNA interactions in spliceosome assembly, possibly ensuring the correct directionality of these events. Previous ArticleNext Article Volume 11Issue 101 October 1992In this issue RelatedDetailsLoading ..." @default.
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• W979014048 title "Roles of PRP8 protein in the assembly of splicing complexes." @default.
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• W979014048 doi "https://doi.org/10.1002/j.1460-2075.1992.tb05457.x" @default.
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