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Gene Review

PRP8  -  U4/U6-U5 snRNP complex component PRP8

Saccharomyces cerevisiae S288c

Synonyms: DBF3, DNA39, Pre-mRNA-splicing factor 8, RNA8, SLT21, ...
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High impact information on PRP8

  • The PRP8 protein is a component of the U5 snRNP and associates with the U4/U6 snRNAs/snRNP to form a multi-snRNP particle believed to be important for spliceosome assembly [1].
  • By using antibodies against the yeast PRP8 protein, a pre-mRNA splicing factor of relative molecular mass 280,000 (Mr280K) stably associated with U5 small nuclear ribonucleoproteins (snRNPs), we have now identified an immunologically related protein in HeLa cell nuclear extracts [2].
  • The striking proximity of two of the prp8 suppressor mutations to the site of the 5'SS:hPrp8 cross-link suggests that some protein:5'SS contacts made before the first step may be subsequently extended to accommodate the 3'SS for the second catalytic step [3].
  • By isolating mutants that eliminate the normal preference for uridine-containing 3' splice sites in a cis-competition, we identified a mutation that is an allele of PRP8, prp8-101 [4].
  • In addition, a suppressor of prp28-1 is a mutant allele of PRP8, which encodes a U5 protein, thus linking PRP28 with U5 [5].

Biological context of PRP8


Anatomical context of PRP8

  • PRP8 encodes a highly conserved U5 snRNP protein required for spliceosome assembly and for both catalytic steps of the splicing reaction [8].

Associations of PRP8 with chemical compounds


Physical interactions of PRP8

  • These findings suggest a model whereby Prp22 disrupts an RNA/protein or RNA/RNA interaction in the spliceosome that is normally stabilized by Prp8 [6].
  • Furthermore, we found that both Prp40 WW domains interact with PPxY motifs (where x is any residue) present in peptides derived from the splicing factors BBP and Prp8 [11].

Other interactions of PRP8

  • Moreover, other PRP8 alleles exhibit synthetic lethality with the absence of Prp17p and show a reduced ability to splice an intron bearing an altered 3' splice junction [8].
  • Interestingly, deletion of SKY1 was synthetically lethal with all prp17 mutants tested, but only with specific prp8 alleles in a domain implicated in governing fidelity of 3'AG recognition [12].
  • A genetic screen for suppressors of BS A-to-G mutants, which stall between the two steps, identified Prp8, the highly conserved spliceosomal factor. prp8 suppressors facilitate the second step for multiple intron mutants and interact functionally with first step suppressors, alleles of PRP16 and U6 snRNA [13].
  • Furthermore, additional genetic interactions with U4-cs1 support a two-state model for this RNA conformational switch and implicate another splicing factor, Prp31, in Prp8-mediated spliceosome activation [14].
  • PRP8 protein could be UV-crosslinked to pre-mRNA in PRP2-depleted spliceosomes stalled before initiation of the splicing reaction [15].

Analytical, diagnostic and therapeutic context of PRP8


  1. A suppressor of a yeast splicing mutation (prp8-1) encodes a putative ATP-dependent RNA helicase. Jamieson, D.J., Rahe, B., Pringle, J., Beggs, J.D. Nature (1991) [Pubmed]
  2. Conservation between yeast and man of a protein associated with U5 small nuclear ribonucleoprotein. Anderson, G.J., Bach, M., Lührmann, R., Beggs, J.D. Nature (1989) [Pubmed]
  3. Functional interactions of Prp8 with both splice sites at the spliceosomal catalytic center. Siatecka, M., Reyes, J.L., Konarska, M.M. Genes Dev. (1999) [Pubmed]
  4. A novel role for a U5 snRNP protein in 3' splice site selection. Umen, J.G., Guthrie, C. Genes Dev. (1995) [Pubmed]
  5. A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene family. Strauss, E.J., Guthrie, C. Genes Dev. (1991) [Pubmed]
  6. 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]
  7. The budding yeast U5 snRNP Prp8 is a highly conserved protein which links RNA splicing with cell cycle progression. Shea, J.E., Toyn, J.H., Johnston, L.H. Nucleic Acids Res. (1994) [Pubmed]
  8. Extensive genetic interactions between PRP8 and PRP17/CDC40, two yeast genes involved in pre-mRNA splicing and cell cycle progression. Ben-Yehuda, S., Russell, C.S., Dix, I., Beggs, J.D., Kupiec, M. Genetics (2000) [Pubmed]
  9. Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activation. Brenner, T.J., Guthrie, C. Genetics (2005) [Pubmed]
  10. Extensive interactions of PRP8 protein with the 5' and 3' splice sites during splicing suggest a role in stabilization of exon alignment by U5 snRNA. Teigelkamp, S., Newman, A.J., Beggs, J.D. EMBO J. (1995) [Pubmed]
  11. Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40. Wiesner, S., Stier, G., Sattler, M., Macias, M.J. J. Mol. Biol. (2002) [Pubmed]
  12. Evidence for a role of Sky1p-mediated phosphorylation in 3' splice site recognition involving both Prp8 and Prp17/Slu4. Dagher, S.F., Fu, X.D. RNA (2001) [Pubmed]
  13. Suppression of multiple substrate mutations by spliceosomal prp8 alleles suggests functional correlations with ribosomal ambiguity mutants. Query, C.C., Konarska, M.M. Mol. Cell (2004) [Pubmed]
  14. Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation. Kuhn, A.N., Reichl, E.M., Brow, D.A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  15. Interaction of the yeast splicing factor PRP8 with substrate RNA during both steps of splicing. Teigelkamp, S., Whittaker, E., Beggs, J.D. Nucleic Acids Res. (1995) [Pubmed]
  16. Dissection of Prp8 protein defines multiple interactions with crucial RNA sequences in the catalytic core of the spliceosome. Turner, I.A., Norman, C.M., Churcher, M.J., Newman, A.J. RNA (2006) [Pubmed]
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