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SKI2  -  SKI complex RNA helicase subunit SKI2

Saccharomyces cerevisiae S288c

Synonyms: Antiviral helicase SKI2, L8084.17, Superkiller protein 2, YLR398C
 
 
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Disease relevance of SKI2

 

High impact information on SKI2

  • These observations suggest that the exosome may be the nucleolytic activity that degrades the body of the mRNA in a 3' to 5' direction, and the exosome's activity on mRNAs may be modulated by Ski2p, Ski3p and Ski8p [2].
  • Thus, the translation apparatus is inherently capable of efficiently using nonpoly(A) mRNA even in the presence of normal amounts of competing poly(A)(+) mRNA, but is normally prevented from doing so by the combined action of the nonessential proteins Ski2p and Slh1p [3].
  • This suggests that Ski2p and Slh1p block translation of non-poly(A) mRNA by an effect on Fun12p, possibly by affecting 60S subunit joining [4].
  • Deletion of RAI1 is synthetically lethal with the rat1-1(ts) mutation and shows genetic interaction with a deletion of SKI2 but not XRN1 [5].
  • The SKI2 antiviral gene represses the copy numbers of the L-A and L-BC viruses and the 20S RNA replicon, apparently by specifically blocking translation of viral RNA [6].
 

Biological context of SKI2

  • The Ski complex (composed of Ski3p, Ski8p, and the DEVH ATPase Ski2p) is a central component of the 3'-5' cytoplasmic mRNA degradation pathway in yeast [7].
  • Identification of gene encoding a putative RNA-helicase, homologous to SKI2, in chromosome VII of Saccharomyces cerevisiae [8].
  • This sequence contains a large open reading frame (ORF) called G9365, coding for a protein of 1967 amino acids that shows a significant homology with the product of the SKI2 gene of S. cerevisiae and contains domains characteristics of RNA-helicases [8].
  • The virus propagation phenotype of mak21-1 is suppressed by ski2 or ski6 mutations, each of which derepresses translation of non-poly(A) mRNA [9].
 

Physical interactions of SKI2

  • Domain interactions within the Ski2/3/8 complex and between the Ski complex and Ski7p [7].
 

Other interactions of SKI2

  • Deletion of two nonessential putative RNA helicases (genes SKI2 and SLH1) makes poly(A) dispensable for translation [4].
  • We propose that Sep1/Xrn1 and Ski2 both act to block translation on transcripts targeted for degradation [10].
  • However, in the absence of Fun12p, eliminating Ski2p and Slh1p shows little enhancement of expression of non-poly(A) mRNA [4].
  • It does so by forming a complex with two partner proteins, Ski2p and Ski3p, which complete a complex that is capable of recruiting and activating the exosome/Ski7p complex that functions in RNA degradation [11].
  • We show that SKI2 encodes a 145-kDa protein with motifs characteristic of helicases and nucleolar proteins and is essential only in cells carrying M dsRNA [12].

References

  1. Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis. Benard, L., Carroll, K., Valle, R.C., Wickner, R.B. Mol. Cell. Biol. (1998) [Pubmed]
  2. The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex. Anderson, J.S., Parker, R.P. EMBO J. (1998) [Pubmed]
  3. 3' poly(A) is dispensable for translation. Searfoss, A.M., Wickner, R.B. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  4. Linking the 3' poly(A) tail to the subunit joining step of translation initiation: relations of Pab1p, eukaryotic translation initiation factor 5b (Fun12p), and Ski2p-Slh1p. Searfoss, A., Dever, T.E., Wickner, R. Mol. Cell. Biol. (2001) [Pubmed]
  5. Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and encodes a protein that binds the nuclear exoribonuclease Rat1p. Xue, Y., Bai, X., Lee, I., Kallstrom, G., Ho, J., Brown, J., Stevens, A., Johnson, A.W. Mol. Cell. Biol. (2000) [Pubmed]
  6. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Masison, D.C., Blanc, A., Ribas, J.C., Carroll, K., Sonenberg, N., Wickner, R.B. Mol. Cell. Biol. (1995) [Pubmed]
  7. Domain interactions within the Ski2/3/8 complex and between the Ski complex and Ski7p. Wang, L., Lewis, M.S., Johnson, A.W. RNA (2005) [Pubmed]
  8. Identification of gene encoding a putative RNA-helicase, homologous to SKI2, in chromosome VII of Saccharomyces cerevisiae. Martegani, E., Vanoni, M., Mauri, I., Rudoni, S., Saliola, M., Alberghina, L. Yeast (1997) [Pubmed]
  9. Mak21p of Saccharomyces cerevisiae, a homolog of human CAATT-binding protein, is essential for 60 S ribosomal subunit biogenesis. Edskes, H.K., Ohtake, Y., Wickner, R.B. J. Biol. Chem. (1998) [Pubmed]
  10. Synthetic lethality of sep1 (xrn1) ski2 and sep1 (xrn1) ski3 mutants of Saccharomyces cerevisiae is independent of killer virus and suggests a general role for these genes in translation control. Johnson, A.W., Kolodner, R.D. Mol. Cell. Biol. (1995) [Pubmed]
  11. The structure of Ski8p, a protein regulating mRNA degradation: Implications for WD protein structure. Madrona, A.Y., Wilson, D.K. Protein Sci. (2004) [Pubmed]
  12. Evidence that the SKI antiviral system of Saccharomyces cerevisiae acts by blocking expression of viral mRNA. Widner, W.R., Wickner, R.B. Mol. Cell. Biol. (1993) [Pubmed]
 
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