Journal
EMBO JOURNAL
Volume 21, Issue 20, Pages 5516-5526Publisher
WILEY
DOI: 10.1093/emboj/cdf555
Keywords
S.pombe; SF1; BBP; U2AF; U2 snRNP; U2/5/6 tri-snRNP
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Funding
- NIGMS NIH HHS [R01 GM025532, GM25532, R01 GM057829, GM57829, R01 GM057829-03] Funding Source: Medline
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We have initiated a biochemical analysis of splicing complexes in extracts from the fission yeast Schizosaccharomyces pombe. Extracts of S.pombe contain high levels of the spliceosome-like U2/5/6 tri-snRNP, which dissociates into mono-snRNPs in the presence of ATP, and supports binding of U2 snRNP to the 3' end of introns, yielding a weak ATP-independent E complex and the stable ATP-dependent complex A. The requirements for S.pombe complex A formation (pre-mRNA sequence elements, protein splicing factors, SF1/BBP and both subunits of U2AF) are analogous to those of mammalian complex A. The S.pombe SF1/BBP, U2AF(59) and U2AF(23) are tightly associated in a novel complex that is required for complex A formation. This pre-formed SF1-U2AF(59)-U2AF(23) complex may represent a streamlined mechanism for recognition of the branch site, pyrimidine tract and 3' splice site at the 3' end of introns.
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