Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. Academic Article uri icon

Overview

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 pre-assembled 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.

publication date

  • April 1, 1998

Research

keywords

  • Fungal Proteins
  • RNA Nucleotidyltransferases
  • RNA Precursors
  • RNA Splicing
  • Saccharomyces cerevisiae Proteins
  • Yeasts

Identity

PubMed Central ID

  • PMC1170553

Scopus Document Identifier

  • 0032055765

Digital Object Identifier (DOI)

  • 10.1093/emboj/17.7.2086

PubMed ID

  • 9524130

Additional Document Info

volume

  • 17

issue

  • 7