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How the Splicing Factors Cus2 and Prp5 Influence Global Splicing Efficiency in Yeast
Author(s) -
Clark Arthur,
Norden Ian,
Hoskins Aaron A.
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.910.6
Subject(s) - rna splicing , snrnp , spliceosome , intron , prp24 , small nuclear rna , biology , splicing factor , minor spliceosome , exonic splicing enhancer , genetics , protein splicing , exon , rna , precursor mrna , microbiology and biotechnology , gene , non coding rna
Splicing is among the most complex biochemical processes in eukaryotic gene expression. Splicing involves the removal of non‐coding introns from pre‐mRNA and the ligation of exons to form mRNA. Splicing is catalyzed by an aggregation of small nuclear ribonucleoproteins (snRNPs) called the spliceosome. Cus2 and Prp5 are two proteins involved in the early steps of splicing. Cus2 is an RNA binding protein that modules conformation of the U2 snRNA. Prp5 is an RNA‐dependent ATPase which is essential for yeast spliceosome assembly by facilitating U2 snRNA basepairing to the intron. ATP hydrolysis by Prp5 is necessary for removal of Cus2 from the U2 snRNP prior to this basepairing, which would imply an antagonistic relationship between Prp5 and Cus2. We are investigating this relationship using RNA‐Seq to study splicing of endogenous yeast introns in Prp5 and Cus2 mutant strains. The initial results indicate that deletion of Cus2 decreases the global splicing efficiency of yeast, particularly the splicing of non‐ribosomal protein pre‐mRNAs. To investigate this further, we have designed RNA‐seq experiments to further test the interplay of Cus2 and Prp5 by employing strains that either contain Cus2 or in which Cus2 was deleted and either contain a wild type Prp5 or an ATPase‐deficient Prp5 mutant. These experiments will identify which yeast pre‐mRNAs are most dependent and most independent of Cus2 and ATP hydrolysis by Prp5 for their splicing.