Prp8: Difference between revisions

Prp8's modified reverse transcritase and RNase H-like domains are postulated to function as recognition, interaction, and handover domains for snRNAs catalytically active in the spliceosome and portions of the pre-mRNA substrate <ref name='Mechanism for aar2p function as a U5 snRNP assembly factor'>PMID:21764848</ref>. Crosslinking experiments have shown that U5 and U6 snRNAs, as well as the GU dinucleotide of the 5' splice site, polypyrimidine tract (close to the intron branch point), and the 3' splice site all interact with or close to the reverse transcriptase and RNase H-like domains of Prp8 which supports the scaffolding and coordination role of Prp8 in pre-mRNA splicing <ref name='Structure and function of an RNase H domain at the heart of the spliceosome'>DOI:10.1038/emboj.2008.209</ref><ref name='splicing factor prp8 governs u4/u6 rna unwinding'>PMID:10024880</ref><ref name='roles of prp8 protein in the assembly of splicing complexes'>PMID:1396567<ref>.