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Gene Review

PRP22  -  DEAH-box ATP-dependent RNA helicase PRP22

Saccharomyces cerevisiae S288c

Synonyms: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22, YER013W
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Disease relevance of PRP22


High impact information on PRP22

  • The predicted PRP22 protein sequence shares extensive homology with that of PRP2 and PRP16 proteins, which are also involved in nuclear pre-mRNA splicing [1].
  • Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes [1].
  • Evidence that helicase activity is important emerged from the analysis of Prp22p motif III (SAT) mutations that uncouple the NTPase and helicase activities [2].
  • We show that Prp22 is required for the second step of actin pre-mRNA splicing [3].
  • Prp22 uses the energy of ATP hydrolysis to effect the release of mRNA from the spliceosome [3].

Biological context of PRP22

  • Expression of HRH1 in a S. cerevisiae prp22 mutant can partially rescue its temperature-sensitive phenotype [4].
  • The predicted amino acid sequence shares extensive homology with Prp2, Prp16, and Prp22 proteins, which are required to splice mRNA precursors in budding yeast [5].
  • Taken together, these results suggest that the 3' splice site of yeast introns is contacted much earlier than previously envisioned by a protein of approximately 120 kDa, and that a transient association of Prp22p with the 3' splice site occurs between the first and second catalytic steps [6].
  • Nonfunctional Prp22 and Prp16 mutants exerted a dominant negative effect on cell growth [7].

Anatomical context of PRP22

  • The product of the yeast PRP22 gene acts late in the splicing of yeast pre-messenger RNA, mediating the release of the spliced mRNA from the spliceosome [1].
  • The hermaphrodite sperm/oocyte switch requires the Caenorhabditis elegans homologs of PRP2 and PRP22 [8].

Associations of PRP22 with chemical compounds

  • Using modified substrates to either mutationally or chemically block the second step, we found that the association of Prp22p with the lariat intermediate represents an authentic transient intermediate and appears to be restricted to the last eight intron nucleotides [9].
  • The arginine/serine-rich domain (RS domain) of HRH1, which is missing in Prp22, confers a nuclear localization signal, and appears to facilitate the interaction of HRH1 with the spliceosome [10].
  • All of the identified antigens, including the human homolog of yeast Prp22 (HRH1), contain a similar structural element characterized by arginine alternating with serine, glutamate, and/or aspartate [11].

Physical interactions of PRP22

  • These findings suggest a model whereby Prp22 disrupts an RNA/protein or RNA/RNA interaction in the spliceosome that is normally stabilized by Prp8 [12].

Other interactions of PRP22

  • Replacing Arg-1753 of Prp8 by either Lys, Ala, Gln, or Glu resulted in suppression of helicase-defective Prp22 mutants [12].
  • Three DEAD/H box proteins, Prp16p, Prp22p and Prp44p, have previously been shown to affect U4/U6 unwinding activity in vitro [13].
  • PRP22 is adjacent to PRE1, whose chromosomal location is currently unknown [14].
  • To illuminate the mechanism of Prp22-catalyzed mRNA release, we performed a genetic screen to identify extragenic suppressors of the cold-sensitive growth defect of a helicase/release-defective Prp22 mutant [12].
  • Recently, mammalian homologues of Prp43p and Prp22p have been described, supporting the idea that splicing in yeast and man is phylogenetically conserved [15].


  1. Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Company, M., Arenas, J., Abelson, J. Nature (1991) [Pubmed]
  2. RNA helicase dynamics in pre-mRNA splicing. Schwer, B., Meszaros, T. EMBO J. (2000) [Pubmed]
  3. Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. Schwer, B., Gross, C.H. EMBO J. (1998) [Pubmed]
  4. Identification of a putative RNA helicase (HRH1), a human homolog of yeast Prp22. Ono, Y., Ohno, M., Shimura, Y. Mol. Cell. Biol. (1994) [Pubmed]
  5. Cloning and characterization of a putative human RNA helicase gene of the DEAH-box protein family. Imamura, O., Sugawara, M., Furuichi, Y. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  6. Interaction of the yeast DExH-box RNA helicase prp22p with the 3' splice site during the second step of nuclear pre-mRNA splicing. McPheeters, D.S., Schwer, B., Muhlenkamp, P. Nucleic Acids Res. (2000) [Pubmed]
  7. Characterization of dominant-negative mutants of the DEAH-box splicing factors Prp22 and Prp16. Schneider, S., Hotz, H.R., Schwer, B. J. Biol. Chem. (2002) [Pubmed]
  8. The hermaphrodite sperm/oocyte switch requires the Caenorhabditis elegans homologs of PRP2 and PRP22. Puoti, A., Kimble, J. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  9. Spatial organization of protein-RNA interactions in the branch site-3' splice site region during pre-mRNA splicing in yeast. McPheeters, D.S., Muhlenkamp, P. Mol. Cell. Biol. (2003) [Pubmed]
  10. A human RNA helicase-like protein, HRH1, facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. Ohno, M., Shimura, Y. Genes Dev. (1996) [Pubmed]
  11. A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors. Neugebauer, K.M., Stolk, J.A., Roth, M.B. J. Cell Biol. (1995) [Pubmed]
  12. Motifs IV and V in the DEAH box splicing factor Prp22 are important for RNA unwinding, and helicase-defective Prp22 mutants are suppressed by Prp8. Schneider, S., Campodonico, E., Schwer, B. J. Biol. Chem. (2004) [Pubmed]
  13. The first ATPase domain of the yeast 246-kDa protein is required for in vivo unwinding of the U4/U6 duplex. Kim, D.H., Rossi, J.J. RNA (1999) [Pubmed]
  14. Mapping the putative RNA helicase genes by sequence overlapping. Chang, T.H., Baum, B. Yeast (1992) [Pubmed]
  15. The mammalian homologue of Prp16p is overexpressed in a cell line tolerant to Leflunomide, a new immunoregulatory drug effective against rheumatoid arthritis. Ortlepp, D., Laggerbauer, B., Müllner, S., Achsel, T., Kirschbaum, B., Lührmann, R. RNA (1998) [Pubmed]
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