Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing Journal Article


Authors: Schwer, B.; Gross, C. H.
Article Title: Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing
Abstract: In order to assess the role of Prp22 in yeast pre-mRNA splicing, we have purified the 130 kDa Prp22 protein and developed an in vitro depletion/reconstitution assay. We show that Prp22 is required for the second step of actin pre-mRNA splicing. Prp22 can act on preassembled spliceosomes that are arrested after step 1 in an ATP-independent fashion. The requirement for Prp22 during step 2 depends on the distance between the branchpoint and the 3' splice site, suggesting a previously unrecognized role for Prp22 in splice site selection. We characterize the biochemical activities of Prp22, a member of the DExH-box family of proteins, and we show that purified recombinant Prp22 protein is an RNA-dependent ATPase and an ATP-dependent RNA helicase. Prp22 uses the energy of ATP hydrolysis to effect the release of mRNA from the spliceosome. Thus, Prp22 has two distinct functions in yeast pre-mRNA splicing: an ATP-independent role during the second catalytic step and an ATP-requiring function in disassembly of the spliceosome.
Keywords: controlled study; unclassified drug; nonhuman; actin; dead-box rna helicases; recombinant fusion proteins; protein purification; recombinant protein; yeast; saccharomyces cerevisiae proteins; adenosine triphosphate; spliceosome; protein family; actins; adenosine triphosphatase; rna helicase; rna helicases; adenosine triphosphatases; hydrolysis; rna splicing; rna precursors; rna, fungal; yeasts; fungal proteins; atpase; spliceosomes; rna nucleotidyltransferases; priority journal; article; dexh-box; prp22; protein prp22
Journal Title: EMBO Journal
Volume: 17
Issue: 7
ISSN: 0261-4189
Publisher: Wiley Blackwell  
Date Published: 1998-04-01
Start Page: 2086
End Page: 2094
Language: English
DOI: 10.1093/emboj/17.7.2086
PUBMED: 9524130
PROVIDER: scopus
PMCID: PMC1170553
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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  1. Christian H Gross
    12 Gross