Skip to main content
NCBI home page
RNA logoLink to RNA
. 2001 Nov;7(11):1566–1577.

A cis-acting element known to block 3' mRNA degradation enhances expression of polyA-minus mRNA in wild-type yeast cells and phenocopies a ski mutant.

J T Brown 1, A W Johnson 1
PMCID: PMC1370199  PMID: 11720286

Abstract

mRNA lacking a 3' polyA tail is not translated efficiently in wild-type eukaryotic cells, but is translated efficiently in yeast ski mutants. This enhanced expression could be due to altered translational specificity. However, as the SKI genes are required for 3' mRNA degradation, it could be a consequence of inhibition of 3' mRNA decay. Therefore, we asked if inhibition of 3' decay of a polyA-minus mRNA in cis would allow its efficient expression in wild-type cells. Capped in vitro reporter transcripts were prepared with or without a 3' cis-acting element known to inhibit 3' degradation (oligoG) and electroporated into yeast cells. The addition of oligoG to a polyA-minus mRNA enhanced expression 30-fold in wild-type cells. This level of expression was the same as that for an oligoG-minus, polyA-minus transcript in a ski mutant. The addition of oligoG did not significantly enhance the expression of polyA-minus mRNA in a ski mutant. The oligoG-dependent increase in expression was due to an increase in initial rate of translation and an increase in the functional half-life of the mRNA, similar to the effects observed in a ski mutant. The enhanced expression of the oligoG-containing RNA did not require Pab1p. We conclude that the enhanced translation of polyA-minus RNA in a ski mutant is due to inhibition of 3' mRNA degradation. Furthermore, a polyA-minus mRNA is expressed in wild-type cells when terminated in an element known to inhibit 3' decay in cis.

Full Text

The Full Text of this article is available as a PDF (475.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P. The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases. Genes Dev. 1999 Aug 15;13(16):2148–2158. doi: 10.1101/gad.13.16.2148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anderson J. S., Parker R. P. 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. EMBO J. 1998 Mar 2;17(5):1497–1506. doi: 10.1093/emboj/17.5.1497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Barabino S. M., Keller W. Last but not least: regulated poly(A) tail formation. Cell. 1999 Oct 1;99(1):9–11. doi: 10.1016/s0092-8674(00)80057-4. [DOI] [PubMed] [Google Scholar]
  4. Benard L., Carroll K., Valle R. C., Masison D. C., Wickner R. B. The ski7 antiviral protein is an EF1-alpha homolog that blocks expression of non-Poly(A) mRNA in Saccharomyces cerevisiae. J Virol. 1999 Apr;73(4):2893–2900. doi: 10.1128/jvi.73.4.2893-2900.1999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Benard L., Carroll K., Valle R. C., Wickner R. B. Ski6p is a homolog of RNA-processing enzymes that affects translation of non-poly(A) mRNAs and 60S ribosomal subunit biogenesis. Mol Cell Biol. 1998 May;18(5):2688–2696. doi: 10.1128/mcb.18.5.2688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Boeck R., Lapeyre B., Brown C. E., Sachs A. B. Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant. Mol Cell Biol. 1998 Sep;18(9):5062–5072. doi: 10.1128/mcb.18.9.5062. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bouveret E., Rigaut G., Shevchenko A., Wilm M., Séraphin B. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 2000 Apr 3;19(7):1661–1671. doi: 10.1093/emboj/19.7.1661. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Brodsky A. S., Silver P. A. Pre-mRNA processing factors are required for nuclear export. RNA. 2000 Dec;6(12):1737–1749. doi: 10.1017/s1355838200001059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Brown J. T., Bai X., Johnson A. W. The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in vivo. RNA. 2000 Mar;6(3):449–457. doi: 10.1017/s1355838200991787. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Burd C. G., Matunis E. L., Dreyfuss G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol Cell Biol. 1991 Jul;11(7):3419–3424. doi: 10.1128/mcb.11.7.3419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Caponigro G., Parker R. Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast. Genes Dev. 1995 Oct 1;9(19):2421–2432. doi: 10.1101/gad.9.19.2421. [DOI] [PubMed] [Google Scholar]
  12. Carroll K., Wickner R. B. Translation and M1 double-stranded RNA propagation: MAK18 = RPL41B and cycloheximide curing. J Bacteriol. 1995 May;177(10):2887–2891. doi: 10.1128/jb.177.10.2887-2891.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Colgan D. F., Manley J. L. Mechanism and regulation of mRNA polyadenylation. Genes Dev. 1997 Nov 1;11(21):2755–2766. doi: 10.1101/gad.11.21.2755. [DOI] [PubMed] [Google Scholar]
  14. Coller J. M., Gray N. K., Wickens M. P. mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation. Genes Dev. 1998 Oct 15;12(20):3226–3235. doi: 10.1101/gad.12.20.3226. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Couttet P., Fromont-Racine M., Steel D., Pictet R., Grange T. Messenger RNA deadenylylation precedes decapping in mammalian cells. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5628–5633. doi: 10.1073/pnas.94.11.5628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Cullen B. R. Nuclear RNA export pathways. Mol Cell Biol. 2000 Jun;20(12):4181–4187. doi: 10.1128/mcb.20.12.4181-4187.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Custódio N., Carmo-Fonseca M., Geraghty F., Pereira H. S., Grosveld F., Antoniou M. Inefficient processing impairs release of RNA from the site of transcription. EMBO J. 1999 May 17;18(10):2855–2866. doi: 10.1093/emboj/18.10.2855. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Decker C. J., Parker R. A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation. Genes Dev. 1993 Aug;7(8):1632–1643. doi: 10.1101/gad.7.8.1632. [DOI] [PubMed] [Google Scholar]
  19. Decker C. J. The exosome: a versatile RNA processing machine. Curr Biol. 1998 Mar 26;8(7):R238–R240. doi: 10.1016/s0960-9822(98)70149-6. [DOI] [PubMed] [Google Scholar]
  20. Eckner R., Ellmeier W., Birnstiel M. L. Mature mRNA 3' end formation stimulates RNA export from the nucleus. EMBO J. 1991 Nov;10(11):3513–3522. doi: 10.1002/j.1460-2075.1991.tb04915.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Edskes H. K., Ohtake Y., Wickner R. B. Mak21p of Saccharomyces cerevisiae, a homolog of human CAATT-binding protein, is essential for 60 S ribosomal subunit biogenesis. J Biol Chem. 1998 Oct 30;273(44):28912–28920. doi: 10.1074/jbc.273.44.28912. [DOI] [PubMed] [Google Scholar]
  22. Everett J. G., Gallie D. R. RNA delivery in Saccharomyces cerevisiae using electroporation. Yeast. 1992 Dec;8(12):1007–1014. doi: 10.1002/yea.320081203. [DOI] [PubMed] [Google Scholar]
  23. Gallie D. R. A tale of two termini: a functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene. 1998 Aug 17;216(1):1–11. doi: 10.1016/s0378-1119(98)00318-7. [DOI] [PubMed] [Google Scholar]
  24. Gallie D. R. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 1991 Nov;5(11):2108–2116. doi: 10.1101/gad.5.11.2108. [DOI] [PubMed] [Google Scholar]
  25. Graber J. H., Cantor C. R., Mohr S. C., Smith T. F. Genomic detection of new yeast pre-mRNA 3'-end-processing signals. Nucleic Acids Res. 1999 Feb 1;27(3):888–894. doi: 10.1093/nar/27.3.888. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Gray N. K., Coller J. M., Dickson K. S., Wickens M. Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 2000 Sep 1;19(17):4723–4733. doi: 10.1093/emboj/19.17.4723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. He W., Parker R. Analysis of mRNA decay pathways in Saccharomyces cerevisiae. Methods. 1999 Jan;17(1):3–10. doi: 10.1006/meth.1998.0701. [DOI] [PubMed] [Google Scholar]
  28. He W., Parker R. Functions of Lsm proteins in mRNA degradation and splicing. Curr Opin Cell Biol. 2000 Jun;12(3):346–350. doi: 10.1016/s0955-0674(00)00098-3. [DOI] [PubMed] [Google Scholar]
  29. Hilleren P., Parker R. Defects in the mRNA export factors Rat7p, Gle1p, Mex67p, and Rat8p cause hyperadenylation during 3'-end formation of nascent transcripts. RNA. 2001 May;7(5):753–764. doi: 10.1017/s1355838201010147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Hilleren P., Parker R. Mechanisms of mRNA surveillance in eukaryotes. Annu Rev Genet. 1999;33:229–260. doi: 10.1146/annurev.genet.33.1.229. [DOI] [PubMed] [Google Scholar]
  31. Hosfield D. J., Mol C. D., Shen B., Tainer J. A. Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell. 1998 Oct 2;95(1):135–146. doi: 10.1016/s0092-8674(00)81789-4. [DOI] [PubMed] [Google Scholar]
  32. Hsu C. L., Stevens A. Yeast cells lacking 5'-->3' exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5' cap structure. Mol Cell Biol. 1993 Aug;13(8):4826–4835. doi: 10.1128/mcb.13.8.4826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Huang Y., Carmichael G. G. Role of polyadenylation in nucleocytoplasmic transport of mRNA. Mol Cell Biol. 1996 Apr;16(4):1534–1542. doi: 10.1128/mcb.16.4.1534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Iizuka N., Najita L., Franzusoff A., Sarnow P. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol Cell Biol. 1994 Nov;14(11):7322–7330. doi: 10.1128/mcb.14.11.7322. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Iizuka N., Sarnow P. Translation-competent extracts from Saccharomyces cerevisiae: effects of L-A RNA, 5' cap, and 3' poly(A) tail on translational efficiency of mRNAs. Methods. 1997 Apr;11(4):353–360. doi: 10.1006/meth.1996.0433. [DOI] [PubMed] [Google Scholar]
  36. Johnson A. W., Kolodner R. D. 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. Mol Cell Biol. 1995 May;15(5):2719–2727. doi: 10.1128/mcb.15.5.2719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Long R. M., Elliott D. J., Stutz F., Rosbash M., Singer R. H. Spatial consequences of defective processing of specific yeast mRNAs revealed by fluorescent in situ hybridization. RNA. 1995 Dec;1(10):1071–1078. [PMC free article] [PubMed] [Google Scholar]
  38. Lopez P. J., Marchand I., Joyce S. A., Dreyfus M. The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo. Mol Microbiol. 1999 Jul;33(1):188–199. doi: 10.1046/j.1365-2958.1999.01465.x. [DOI] [PubMed] [Google Scholar]
  39. Masison D. C., Blanc A., Ribas J. C., Carroll K., Sonenberg N., Wickner R. B. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763–2771. doi: 10.1128/mcb.15.5.2763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Mitchell P., Petfalski E., Shevchenko A., Mann M., Tollervey D. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases. Cell. 1997 Nov 14;91(4):457–466. doi: 10.1016/s0092-8674(00)80432-8. [DOI] [PubMed] [Google Scholar]
  41. Mitchell P., Tollervey D. Musing on the structural organization of the exosome complex. Nat Struct Biol. 2000 Oct;7(10):843–846. doi: 10.1038/82817. [DOI] [PubMed] [Google Scholar]
  42. Muhlrad D., Decker C. J., Parker R. Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5'-->3' digestion of the transcript. Genes Dev. 1994 Apr 1;8(7):855–866. doi: 10.1101/gad.8.7.855. [DOI] [PubMed] [Google Scholar]
  43. Muhlrad D., Decker C. J., Parker R. Turnover mechanisms of the stable yeast PGK1 mRNA. Mol Cell Biol. 1995 Apr;15(4):2145–2156. doi: 10.1128/mcb.15.4.2145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Niepel M., Ling J., Gallie D. R. Secondary structure in the 5'-leader or 3'-untranslated region reduces protein yield but does not affect the functional interaction between the 5'-cap and the poly(A) tail. FEBS Lett. 1999 Nov 26;462(1-2):79–84. doi: 10.1016/s0014-5793(99)01514-8. [DOI] [PubMed] [Google Scholar]
  45. Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N., Yanagida M., He X., Mueller U., Sazer S. Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1. EMBO J. 1996 Oct 15;15(20):5595–5605. [PMC free article] [PubMed] [Google Scholar]
  46. Ohtake Y., Wickner R. B. KRB1, a suppressor of mak7-1 (a mutant RPL4A), is RPL4B, a second ribosomal protein L4 gene, on a fragment of Saccharomyces chromosome XII. Genetics. 1995 May;140(1):129–137. doi: 10.1093/genetics/140.1.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Ohtake Y., Wickner R. B. Yeast virus propagation depends critically on free 60S ribosomal subunit concentration. Mol Cell Biol. 1995 May;15(5):2772–2781. doi: 10.1128/mcb.15.5.2772. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Peltz S. W., Hammell A. B., Cui Y., Yasenchak J., Puljanowski L., Dinman J. D. Ribosomal protein L3 mutants alter translational fidelity and promote rapid loss of the yeast killer virus. Mol Cell Biol. 1999 Jan;19(1):384–391. doi: 10.1128/mcb.19.1.384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Poole T. L., Stevens A. Structural modifications of RNA influence the 5' exoribonucleolytic hydrolysis by XRN1 and HKE1 of Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1997 Jun 27;235(3):799–805. doi: 10.1006/bbrc.1997.6877. [DOI] [PubMed] [Google Scholar]
  50. Proweller A., Butler J. S. Ribosome concentration contributes to discrimination against poly(A)- mRNA during translation initiation in Saccharomyces cerevisiae. J Biol Chem. 1997 Feb 28;272(9):6004–6010. doi: 10.1074/jbc.272.9.6004. [DOI] [PubMed] [Google Scholar]
  51. Proweller A., Butler S. Efficient translation of poly(A)-deficient mRNAs in Saccharomyces cerevisiae. Genes Dev. 1994 Nov 1;8(21):2629–2640. doi: 10.1101/gad.8.21.2629. [DOI] [PubMed] [Google Scholar]
  52. Sachs A. B., Davis R. W., Kornberg R. D. A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol Cell Biol. 1987 Sep;7(9):3268–3276. doi: 10.1128/mcb.7.9.3268. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Sachs A. B., Davis R. W. The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell. 1989 Sep 8;58(5):857–867. doi: 10.1016/0092-8674(89)90938-0. [DOI] [PubMed] [Google Scholar]
  54. Sachs A. B., Sarnow P., Hentze M. W. Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell. 1997 Jun 13;89(6):831–838. doi: 10.1016/s0092-8674(00)80268-8. [DOI] [PubMed] [Google Scholar]
  55. Searfoss A. M., Wickner R. B. 3' poly(A) is dispensable for translation. Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):9133–9137. doi: 10.1073/pnas.97.16.9133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
  57. Tanguay R. L., Gallie D. R. The effect of the length of the 3'-untranslated region on expression in plants. FEBS Lett. 1996 Oct 7;394(3):285–288. doi: 10.1016/0014-5793(96)00970-2. [DOI] [PubMed] [Google Scholar]
  58. Tanguay R. L., Gallie D. R. Translational efficiency is regulated by the length of the 3' untranslated region. Mol Cell Biol. 1996 Jan;16(1):146–156. doi: 10.1128/mcb.16.1.146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Tarun S. Z., Jr, Wells S. E., Deardorff J. A., Sachs A. B. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9046–9051. doi: 10.1073/pnas.94.17.9046. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Tharun S., He W., Mayes A. E., Lennertz P., Beggs J. D., Parker R. Yeast Sm-like proteins function in mRNA decapping and decay. Nature. 2000 Mar 30;404(6777):515–518. doi: 10.1038/35006676. [DOI] [PubMed] [Google Scholar]
  61. Toh-E A., Guerry P., Wickner R. B. Chromosomal superkiller mutants of Saccharomyces cerevisiae. J Bacteriol. 1978 Dec;136(3):1002–1007. doi: 10.1128/jb.136.3.1002-1007.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Toh-E A., Wickner R. B. "Superkiller" mutations suppress chromosomal mutations affecting double-stranded RNA killer plasmid replication in saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1980 Jan;77(1):527–530. doi: 10.1073/pnas.77.1.527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Tucker M., Parker R. Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae. Annu Rev Biochem. 2000;69:571–595. doi: 10.1146/annurev.biochem.69.1.571. [DOI] [PubMed] [Google Scholar]
  64. Vende P., Piron M., Castagné N., Poncet D. Efficient translation of rotavirus mRNA requires simultaneous interaction of NSP3 with the eukaryotic translation initiation factor eIF4G and the mRNA 3' end. J Virol. 2000 Aug;74(15):7064–7071. doi: 10.1128/jvi.74.15.7064-7071.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Wang Z., Kiledjian M. Identification of an erythroid-enriched endoribonuclease activity involved in specific mRNA cleavage. EMBO J. 2000 Jan 17;19(2):295–305. doi: 10.1093/emboj/19.2.295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Wickner R. B. Prions and RNA viruses of Saccharomyces cerevisiae. Annu Rev Genet. 1996;30:109–139. doi: 10.1146/annurev.genet.30.1.109. [DOI] [PubMed] [Google Scholar]
  67. Wickner R. B., Ridley S. P., Fried H. M., Ball S. G. Ribosomal protein L3 is involved in replication or maintenance of the killer double-stranded RNA genome of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1982 Aug;79(15):4706–4708. doi: 10.1073/pnas.79.15.4706. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Widner W. R., Wickner R. B. Evidence that the SKI antiviral system of Saccharomyces cerevisiae acts by blocking expression of viral mRNA. Mol Cell Biol. 1993 Jul;13(7):4331–4341. doi: 10.1128/mcb.13.7.4331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Williamson J. R., Raghuraman M. K., Cech T. R. Monovalent cation-induced structure of telomeric DNA: the G-quartet model. Cell. 1989 Dec 1;59(5):871–880. doi: 10.1016/0092-8674(89)90610-7. [DOI] [PubMed] [Google Scholar]
  70. Wilusz C. J., Wormington M., Peltz S. W. The cap-to-tail guide to mRNA turnover. Nat Rev Mol Cell Biol. 2001 Apr;2(4):237–246. doi: 10.1038/35067025. [DOI] [PubMed] [Google Scholar]
  71. van Hoof A., Lennertz P., Parker R. Yeast exosome mutants accumulate 3'-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs. Mol Cell Biol. 2000 Jan;20(2):441–452. doi: 10.1128/mcb.20.2.441-452.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. van Hoof A., Parker R. The exosome: a proteasome for RNA? Cell. 1999 Nov 12;99(4):347–350. doi: 10.1016/s0092-8674(00)81520-2. [DOI] [PubMed] [Google Scholar]
  73. van Hoof A., Staples R. R., Baker R. E., Parker R. Function of the ski4p (Csl4p) and Ski7p proteins in 3'-to-5' degradation of mRNA. Mol Cell Biol. 2000 Nov;20(21):8230–8243. doi: 10.1128/mcb.20.21.8230-8243.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from RNA are provided here courtesy of The RNA Society

RESOURCES