Extensive interactions of PRP8 protein with the 5' and 3' splice sites during splicing suggest a role in stabilization of exon alignment by U5 snRNA
作者： S. Teigelkamp , A.J. Newman , J.D. Beggs
DOI: 10.1002/J.1460-2075.1995.TB07258.X
关键词:
摘要: Precursor RNAs containing 4-thiouridine at specific sites were used with UV-crosslinking to map the binding of yeast protein splicing factor PRP8. PRP8 interacts a region least eight exon nucleotides 5' splice site and minimum 13 part polypyrimidine tract in 3' region. Crosslinking mutant duplicated indicated that interaction is not sequence specific, nor does it depend on being functional. Binding was established before step 1 after splicing. These interactions place close proposed catalytic core spliceosome during both transesterification reactions. To date, this represents most extensive mapping site(s) substrate RNA. We propose large stabilize intrinsically weaker U5 snRNA exons for alignment by snRNP.
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