Release Factor eRF3 Mediates Premature Translation Termination on Polylysine-Stalled Ribosomes in Saccharomyces cerevisiae

REFERENCES

• Klauer AA, van Hoof A. 2012. Degradation of mRNAs that lack a stop codon: a decade of nonstop progress. Wiley Interdiscip. Rev. RNA 3:649–660. http://dx.doi.org/10.1002/wrna.1124.
   PubMedGoogle Scholar
• Inada T. 2013. Quality control systems for aberrant mRNAs induced by aberrant translation elongation and termination. Biochim. Biophys. Acta 1829:634–642. http://dx.doi.org/10.1016/j.bbagrm.2013.02.004.
   PubMedGoogle Scholar
• Parker R. 2012. RNA degradation in Saccharomyces cerevisiae. Genetics 191:671–702. http://dx.doi.org/10.1534/genetics.111.137265.
   PubMed Web of Science ®Google Scholar
• Graber JH, Cantor CR, Mohr SC, Smith TF. 1999. Genomic detection of new yeast pre-mRNA 3′-end-processing signals. Nucleic Acids Res. 27:888–894. http://dx.doi.org/10.1093/nar/27.3.888.
   PubMed Web of Science ®Google Scholar
• Akimitsu N. 2008. Messenger RNA surveillance systems monitoring proper translation termination. J. Biochem. 143:1–8. http://dx.doi.org/10.1093/jb/mvm204.
   PubMedGoogle Scholar
• Inada T, Aiba H. 2005. Translation of aberrant mRNAs lacking a termination codon or with a shortened 3′-UTR is repressed after initiation in yeast. EMBO J. 24:1584–1595. http://dx.doi.org/10.1038/sj.emboj.7600636.
   PubMedGoogle Scholar
• Rodrigo-Brenni MC, Hegde RS. 2012. Design principles of protein biosynthesis-coupled quality control. Dev. Cell 23:896–907. http://dx.doi.org/10.1016/j.devcel.2012.10.012.
   PubMedGoogle Scholar
• Ito-Harashima S, Kuroha K, Tatematsu T, Inada T. 2007. Translation of the poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast. Genes Dev. 21:519–524. http://dx.doi.org/10.1101/gad.1490207.
   PubMed Web of Science ®Google Scholar
• Dimitrova LN, Kuroha K, Tatematsu T, Inada T. 2009. Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J. Biol. Chem. 284:10343–10352. http://dx.doi.org/10.1074/jbc.M808840200.
   PubMed Web of Science ®Google Scholar
• Lu J, Deutsch C. 2008. Electrostatics in the ribosomal tunnel modulate chain elongation rates. J. Mol. Biol. 384:73–86. http://dx.doi.org/10.1016/j.jmb.2008.08.089.
   PubMed Web of Science ®Google Scholar
• Brandman O, Stewart-Ornstein J, Wong D, Larson A, Williams CC, Li GW, Zhou S, King D, Shen PS, Weibezahn J, Dunn JG, Rouskin S, Inada T, Frost A, Weissman JS. 2012. A ribosome-bound quality control complex triggers degradation of nascent peptides and signals translation stress. Cell 151:1042–1054. http://dx.doi.org/10.1016/j.cell.2012.10.044.
   PubMed Web of Science ®Google Scholar
• Bhushan S, Meyer H, Starosta AL, Becker T, Mielke T, Berninghausen O, Sattler M, Wilson DN, Beckmann R. 2010. Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide. Mol. Cell 40:138–146. http://dx.doi.org/10.1016/j.molcel.2010.09.009.
   PubMed Web of Science ®Google Scholar
• Wei J, Wu C, Sachs MS. 2012. The arginine attenuator peptide interferes with the ribosome peptidyl transferase center. Mol. Cell. Biol. 32:2396–2406. http://dx.doi.org/10.1128/MCB.00136-12.
   PubMed Web of Science ®Google Scholar
• Adams DR, Ron D, Kiely PA. 2011. RACK1, a multifaceted scaffolding protein: structure and function. Cell Commun. Signal. 9:22. http://dx.doi.org/10.1186/1478-811X-9-22.
   PubMed Web of Science ®Google Scholar
• Kuroha K, Akamatsu M, Dimitrova L, Ito T, Kato Y, Shirahige K, Inada T. 2010. Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep. 11:956–961. http://dx.doi.org/10.1038/embor.2010.169.
   PubMedGoogle Scholar
• Bengtson MH, Joazeiro CA. 2010. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467:470–473. http://dx.doi.org/10.1038/nature09371.
   PubMed Web of Science ®Google Scholar
• Defenouillere Q, Yao Y, Mouaikel J, Namane A, Galopier A, Decourty L, Doyen A, Malabat C, Saveanu C, Jacquier A, Fromont-Racine M. 2013. Cdc48-associated complex bound to 60S particles is required for the clearance of aberrant translation products. Proc. Natl. Acad. Sci. U. S. A. 110:5046–5051. http://dx.doi.org/10.1073/pnas.1221724110.
   PubMed Web of Science ®Google Scholar
• Shao S, von der Malsburg K, Hegde RS. 2013. Listerin-dependent nascent protein ubiquitination relies on ribosome subunit dissociation. Mol. Cell 50:637–648. http://dx.doi.org/10.1016/j.molcel.2013.04.015.
   PubMed Web of Science ®Google Scholar
• Verma R, Oania RS, Kolawa NJ, Deshaies RJ. 2013. Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. eLife 2:e00308. http://dx.doi.org/10.7554/eLife.00308.
   PubMed Web of Science ®Google Scholar
• Doma MK, Parker R. 2006. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 440:561–564. http://dx.doi.org/10.1038/nature04530.
   PubMed Web of Science ®Google Scholar
• Tsuboi T, Kuroha K, Kudo K, Makino S, Inoue E, Kashima I, Inada T. 2012. Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3′ end of aberrant mRNA. Mol. Cell 46:518–529. http://dx.doi.org/10.1016/j.molcel.2012.03.013.
   PubMed Web of Science ®Google Scholar
• Harigaya Y, Parker R. 2010. No-go decay: a quality control mechanism for RNA in translation. Wiley Interdiscip. Rev. RNA 1:132–141.
   PubMed Web of Science ®Google Scholar
• Rospert S, Rakwalska M, Dubaquié Y. 2005. Polypeptide chain termination and stop codon readthrough on eukaryotic ribosomes. Rev. Physiol. Biochem. Pharmacol. 155:1–30. http://dx.doi.org/10.1007/3-540-28217-3_1.
   PubMed Web of Science ®Google Scholar
• Dever TE, Green R. 2012. The elongation, termination, and recycling phases of translation in eukaryotes. Cold Spring Harb. Perspect. Biol. 4:a013706. http://dx.doi.org/10.1101/cshperspect.a013706.
   PubMed Web of Science ®Google Scholar
• Franckenberg S, Becker T, Beckmann R. 2012. Structural view on recycling of archaeal and eukaryotic ribosomes after canonical termination and ribosome rescue. Curr. Opin. Struct. Biol. 22:786–796. http://dx.doi.org/10.1016/j.sbi.2012.08.002.
   PubMedGoogle Scholar
• Atkinson GC, Baldauf SL, Hauryliuk V. 2008. Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components. BMC Evol. Biol. 8:290. http://dx.doi.org/10.1186/1471-2148-8-290.
   PubMedGoogle Scholar
• Shoemaker CJ, Green R. 2011. Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc. Natl. Acad. Sci. U. S. A. 108:E1392–E1398. http://dx.doi.org/10.1073/pnas.1113956108.
   PubMed Web of Science ®Google Scholar
• Passos DO, Doma MK, Shoemaker CJ, Muhlrad D, Green R, Weissman J, Hollien J, Parker R. 2009. Analysis of Dom34 and its function in no-go decay. Mol. Biol. Cell 20:3025–3032. http://dx.doi.org/10.1091/mbc.E09-01-0028.
   PubMedGoogle Scholar
• van Hoof A, Frischmeyer PA, Dietz HC, Parker R. 2002. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295:2262–2264. http://dx.doi.org/10.1126/science.1067272.
   PubMed Web of Science ®Google Scholar
• Frischmeyer PA, van Hoof A, O'Donnell K, Guerrerio AL, Parker R, Dietz HC. 2002. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295:2258–2261. http://dx.doi.org/10.1126/science.1067338.
   PubMed Web of Science ®Google Scholar
• Araki Y, Takahashi S, Kobayashi T, Kajiho H, Hoshino S, Katada T. 2001. Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast. EMBO J. 20:4684–4693. http://dx.doi.org/10.1093/emboj/20.17.4684.
   PubMedGoogle Scholar
• Chiabudini M, Conz C, Reckmann F, Rospert S. 2012. RAC/Ssb is required for translational repression induced by polylysine segments within nascent chains. Mol. Cell. Biol. 32:4769–4779. http://dx.doi.org/10.1128/MCB.00809-12.
   PubMedGoogle Scholar
• Peisker K, Chiabudini M, Rospert S. 2010. The ribosome-bound Hsp70 homolog Ssb of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1803:662–672. http://dx.doi.org/10.1016/j.bbamcr.2010.03.005.
   PubMed Web of Science ®Google Scholar
• Gautschi M, Lilie H, Fünfschilling U, Mun A, Ross S, Lithgow T, Rücknagel P, Rospert S. 2001. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc. Natl. Acad. Sci. U. S. A. 98:3762–3767. http://dx.doi.org/10.1073/pnas.071057198.
   PubMedGoogle Scholar
• Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA. 1992. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71:97–105. http://dx.doi.org/10.1016/0092-8674(92)90269-I.
   PubMedGoogle Scholar
• Gautschi M, Mun A, Ross S, Rospert S. 2002. A functional chaperone triad on the yeast ribosome. Proc. Natl. Acad. Sci. U. S. A. 99:4209–4214. http://dx.doi.org/10.1073/pnas.062048599.
   PubMedGoogle Scholar
• Pfund C, Lopez-Hoyo N, Ziegelhoffer T, Schilke BA, Lopez-Buesa P, Walter WA, Wiedmann M, Craig EA. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17:3981–3989. http://dx.doi.org/10.1093/emboj/17.14.3981.
   PubMedGoogle Scholar
• Willmund F, Del Alamo M, Pechmann S, Chen T, Albanese V, Dammer EB, Peng J, Frydman J. 2013. The cotranslational function of ribosome-associated hsp70 in eukaryotic protein homeostasis. Cell 152:196–209. http://dx.doi.org/10.1016/j.cell.2012.12.001.
   PubMedGoogle Scholar
• Huang P, Gautschi M, Walter W, Rospert S, Craig EA. 2005. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat. Struct. Mol. Biol. 12:497–504. http://dx.doi.org/10.1038/nsmb942.
   PubMed Web of Science ®Google Scholar
• Peisker K, Braun D, Wölfle T, Hentschel J, Fünfschilling U, Fischer G, Sickmann A, Rospert S. 2008. Ribosome-associated complex binds to ribosomes in close proximity of Rpl31 at the exit of the polypeptide tunnel in yeast. Mol. Biol. Cell 19:5279–5288. http://dx.doi.org/10.1091/mbc.E08-06-0661.
   PubMedGoogle Scholar
• Leidig C, Bange G, Kopp J, Amlacher S, Aravind A, Wickles S, Witte G, Hurt E, Beckmann R, Sinning I. 2013. Structural characterization of a eukaryotic chaperone-the ribosome-associated complex. Nat. Struct. Mol. Biol. 20:23–28. http://dx.doi.org/10.1038/nsmb.2447.
   PubMedGoogle Scholar
• Koplin A, Preissler S, Ilina Y, Koch M, Scior A, Erhardt M, Deuerling E. 2010. A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J. Cell Biol. 189:57–68. http://dx.doi.org/10.1083/jcb.200910074.
   PubMed Web of Science ®Google Scholar
• Albanese V, Reissmann S, Frydman J. 2010. A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J. Cell Biol. 189:69–81. http://dx.doi.org/10.1083/jcb.201001054.
   PubMed Web of Science ®Google Scholar
• Rakwalska M, Rospert S. 2004. The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol. Cell. Biol. 24:9186–9197. http://dx.doi.org/10.1128/MCB.24.20.9186-9197.2004.
   PubMedGoogle Scholar
• Hatin I, Fabret C, Namy O, Decatur W, Rousset JP. 2007. Fine tuning of translation termination efficiency in Saccharomyces cerevisiae involves two factors in close proximity to the exit tunnel of the ribosome. Genetics 177:1527–1537. http://dx.doi.org/10.1534/genetics.107.070771.
   PubMedGoogle Scholar
• von Plehwe U, Berndt U, Conz C, Chiabudini M, Fitzke E, Sickmann A, Petersen A, Pfeifer D, Rospert S. 2009. The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase network. Genes Dev. 23:2102–2115. http://dx.doi.org/10.1101/gad.529409.
   PubMed Web of Science ®Google Scholar
• Prunuske AJ, Waltner JK, Kuhn P, Gu B, Craig EA. 2012. Role for the molecular chaperones Zuo1 and Ssz1 in quorum sensing via activation of the transcription factor Pdr1. Proc. Natl. Acad. Sci. U. S. A. 109:472–477. http://dx.doi.org/10.1073/pnas.1119184109.
   PubMedGoogle Scholar
• Richly H, Rocha-Viegas L, Ribeiro JD, Demajo S, Gundem G, Lopez-Bigas N, Nakagawa T, Rospert S, Ito T, Di Croce L. 2010. Transcriptional activation of Polycomb-repressed genes by ZRF1. Nature 468:1124–1128. http://dx.doi.org/10.1038/nature09574.
   PubMedGoogle Scholar
• Ribeiro JD, Morey L, Mas A, Gutierrez A, Luis NM, Mejetta S, Richly H, Benitah SA, Keyes WM, Di Croce L. 2013. ZRF1 controls oncogene-induced senescence through the INK4-ARF locus. Oncogene 32:2161–2168.
   PubMedGoogle Scholar
• Heitman J, Movva NR, Hiestand PC, Hall MN. 1991. FK 506-binding protein proline rotamase is a target for the immunosuppressive agent FK 506 in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 88:1948–1952. http://dx.doi.org/10.1073/pnas.88.5.1948.
   PubMed Web of Science ®Google Scholar
• Belyi Y, Tartakovskaya D, Tais A, Fitzke E, Tzivelekidis T, Jank T, Rospert S, Aktories K. 2012. Elongation factor 1A is the target of growth inhibition in yeast caused by Legionella pneumophila glucosyltransferase Lgt1. J. Biol. Chem. 287:26029–26037. http://dx.doi.org/10.1074/jbc.M112.372672.
   PubMed Web of Science ®Google Scholar
• Gietz RD, Sugino A. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527–534. http://dx.doi.org/10.1016/0378-1119(88)90185-0.
   PubMed Web of Science ®Google Scholar
• Meaux S, Van Hoof A. 2006. Yeast transcripts cleaved by an internal ribozyme provide new insight into the role of the cap and poly(A) tail in translation and mRNA decay. RNA 12:1323–1337. http://dx.doi.org/10.1261/rna.46306.
   PubMedGoogle Scholar
• Gari E, Piedrafita L, Aldea M, Herrero E. 1997. A set of vectors with a tetracycline-regulatable promoter system for modulated gene expression in Saccharomyces cerevisiae. Yeast 13:837–848. http://dx.doi.org/10.1002/(SICI)1097-0061(199707)13:9<837::AID-YEA145>3.0.CO;2-T.
   PubMedGoogle Scholar
• Carvin CD, Kladde MP. 2004. Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1–10. J. Biol. Chem. 279:33057–33062. http://dx.doi.org/10.1074/jbc.M405033200.
   PubMed Web of Science ®Google Scholar
• Kushnirov VV. 2000. Rapid and reliable protein extraction from yeast. Yeast 16:857–860. http://dx.doi.org/10.1002/1097-0061(20000630)16:9<857::AID-YEA561>3.0.CO;2-B.
   PubMed Web of Science ®Google Scholar
• Raue U, Oellerer S, Rospert S. 2007. Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence. J. Biol. Chem. 282:7809–7816. http://dx.doi.org/10.1074/jbc.M611436200.
   PubMedGoogle Scholar
• Ashe MP, De Long SK, Sachs AB. 2000. Glucose depletion rapidly inhibits translation initiation in yeast. Mol. Biol. Cell 11:833–848. http://dx.doi.org/10.1091/mbc.11.3.833.
   PubMed Web of Science ®Google Scholar
• Saini P, Eyler DE, Green R, Dever TE. 2009. Hypusine-containing protein eIF5A promotes translation elongation. Nature 459:118–121. http://dx.doi.org/10.1038/nature08034.
   PubMed Web of Science ®Google Scholar
• Fan H, Penman S. 1970. Regulation of protein synthesis in mammalian cells. II. Inhibition of protein synthesis at the level of initiation during mitosis. J. Mol. Biol. 50:655–670.
   PubMedGoogle Scholar
• Schägger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368–379. http://dx.doi.org/10.1016/0003-2697(87)90587-2.
   PubMed Web of Science ®Google Scholar
• Haseloff J, Gerlach WL. 1988. Simple RNA enzymes with new and highly specific endoribonuclease activities. Nature 334:585–591. http://dx.doi.org/10.1038/334585a0.
   PubMed Web of Science ®Google Scholar
• Düvel K, Valerius O, Mangus DA, Jacobson A, Braus GH. 2002. Replacement of the yeast TRP4 3′ untranslated region by a hammerhead ribozyme results in a stable and efficiently exported mRNA that lacks a poly(A) tail. RNA 8:336–344. http://dx.doi.org/10.1017/S1355838202021039.
   PubMedGoogle Scholar
• Shoemaker CJ, Eyler DE, Green R. 2010. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 330:369–372. http://dx.doi.org/10.1126/science.1192430.
   PubMed Web of Science ®Google Scholar
• Matsuda R, Ikeuchi K, Nomura S, Inada T. 2014. Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast. Genes Cells 19:1–12. http://dx.doi.org/10.1111/gtc.12106.
   PubMed Web of Science ®Google Scholar
• Ogg SC, Walter P. 1995. SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation. Cell 81:1075–1084. http://dx.doi.org/10.1016/S0092-8674(05)80012-1.
   PubMedGoogle Scholar
• Schneider-Poetsch T, Ju J, Eyler DE, Dang Y, Bhat S, Merrick WC, Green R, Shen B, Liu JO. 2010. Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat. Chem. Biol. 6:209–217.
   PubMed Web of Science ®Google Scholar
• Nielsen PJ, McConkey EH. 1980. Evidence for control of protein synthesis in HeLa cells via the elongation rate. J. Cell Physiol. 104:269–281. http://dx.doi.org/10.1002/jcp.1041040302.
   PubMedGoogle Scholar
• Sivan G, Kedersha N, Elroy-Stein O. 2007. Ribosomal slowdown mediates translational arrest during cellular division. Mol. Cell. Biol. 27:6639–6646. http://dx.doi.org/10.1128/MCB.00798-07.
   PubMed Web of Science ®Google Scholar
• Anand M, Chakraburtty K, Marton MJ, Hinnebusch AG, Kinzy TG. 2003. Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3. J. Biol. Chem. 278:6985–6991. http://dx.doi.org/10.1074/jbc.M209224200.
   PubMedGoogle Scholar
• Stansfield I, Eurwilaichitr L, Akhmaloka Tuite MF. 1996. Depletion in the levels of the release factor eRF1 causes a reduction in the efficiency of translation termination in yeast. Mol. Microbiol. 20:1135–1143. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02634.x.
   PubMed Web of Science ®Google Scholar
• Yan F, Doronina VA, Sharma P, Brown JD. 2010. Orchestrating ribosomal activity from inside: effects of the nascent chain on the peptidyltransferase centre. Biochem. Soc. Trans. 38:1576–1580. http://dx.doi.org/10.1042/BST0381576.
   PubMedGoogle Scholar
• Akimitsu N, Tanaka J, Pelletier J. 2007. Translation of nonSTOP mRNA is repressed post-initiation in mammalian cells. EMBO J. 26:2327–2338. http://dx.doi.org/10.1038/sj.emboj.7601679.
   PubMedGoogle Scholar
• Luke G, Escuin H, De Felipe P, Ryan M. 2010. 2A to the fore – research, technology and applications. Biotechnol. Genet. Eng. Rev. 26:223–260. http://dx.doi.org/10.5661/bger-26-223.
   PubMedGoogle Scholar
• Gerbasi VR, Weaver CM, Hill S, Friedman DB, Link AJ. 2004. Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol. Cell. Biol. 24:8276–8287. http://dx.doi.org/10.1128/MCB.24.18.8276-8287.2004.
   PubMedGoogle Scholar
• Kurata S, Shen B, Liu JO, Takeuchi N, Kaji A, Kaji H. 2013. Possible steps of complete disassembly of post-termination complex by yeast eEF3 deduced from inhibition by translocation inhibitors. Nucleic Acids Res. 41:264–276. http://dx.doi.org/10.1093/nar/gks958.
   PubMed Web of Science ®Google Scholar
• Doronina VA, Wu C, de Felipe P, Sachs MS, Ryan MD, Brown JD. 2008. Site-specific release of nascent chains from ribosomes at a sense codon. Mol. Cell. Biol. 28:4227–4239. http://dx.doi.org/10.1128/MCB.00421-08.
   PubMed Web of Science ®Google Scholar
• Goloubinoff P, De Los Rios P. 2007. The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem. Sci. 32:372–380. http://dx.doi.org/10.1016/j.tibs.2007.06.008.
   PubMed Web of Science ®Google Scholar
• Shalgi R, Hurt JA, Krykbaeva I, Taipale M, Lindquist S, Burge CB. 2013. Widespread regulation of translation by elongation pausing in heat shock. Mol. Cell 49:439–452. http://dx.doi.org/10.1016/j.molcel.2012.11.028.
   PubMed Web of Science ®Google Scholar
• Liu B, Han Y, Qian SB. 2013. Cotranslational response to proteotoxic stress by elongation pausing of ribosomes. Mol. Cell 49:453–463. http://dx.doi.org/10.1016/j.molcel.2012.12.001.
   PubMed Web of Science ®Google Scholar
• Frydman J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70:603–647. http://dx.doi.org/10.1146/annurev.biochem.70.1.603.
   PubMed Web of Science ®Google Scholar
• Allen KD, Wegrzyn RD, Chernova TA, Muller S, Newnam GP, Winslett PA, Wittich KB, Wilkinson KD, Chernoff YO. 2005. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169:1227–1242.
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Newnam GP, Kumar J, Allen K, Zink AD. 1999. Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion. Mol. Cell. Biol. 19:8103–8112.
   PubMed Web of Science ®Google Scholar
• Shorter J, Lindquist S. 2008. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J. 27:2712–2724. http://dx.doi.org/10.1038/emboj.2008.194.
   PubMed Web of Science ®Google Scholar
• Cherkasova V, Qiu H, Hinnebusch AG. 2010. Snf1 promotes phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 by activating Gcn2 and inhibiting phosphatases Glc7 and Sit4. Mol. Cell. Biol. 30:2862–2873. http://dx.doi.org/10.1128/MCB.00183-10.
   PubMedGoogle Scholar
• Leprivier G, Remke M, Rotblat B, Dubuc A, Mateo AR, Kool M, Agnihotri S, El-Naggar A, Yu B, Somasekharan SP, Faubert B, Bridon G, Tognon CE, Mathers J, Thomas R, Li A, Barokas A, Kwok B, Bowden M, Smith S, Wu X, Korshunov A, Hielscher T, Northcott PA, Galpin JD, Ahern CA, Wang Y, McCabe MG, Collins VP, Jones RG, Pollak M, Delattre O, Gleave ME, Jan E, Pfister SM, Proud CG, Derry WB, Taylor MD, Sorensen PH. 2013. The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation. Cell 153:1064–1079. http://dx.doi.org/10.1016/j.cell.2013.04.055.
   PubMed Web of Science ®Google Scholar
• Hedbacker K, Carlson M. 2008. SNF1/AMPK pathways in yeast. Front. Biosci. 13:2408–2420. http://dx.doi.org/10.2741/2854.
   PubMed Web of Science ®Google Scholar
• Fabret C, Cosnier B, Lekomtsev S, Gillet S, Hatin I, Le Marechal P, Rousset JP. 2008. A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability. BMC Mol. Biol. 9:22. http://dx.doi.org/10.1186/1471-2199-9-22.
   PubMedGoogle Scholar
• Gibson TJ. 2012. RACK1 research - ships passing in the night? FEBS Lett. 586:2787–2789. http://dx.doi.org/10.1016/j.febslet.2012.04.048.
   PubMedGoogle Scholar
• Gandin V, Senft D, Topisirovic I, Ronai ZA. 2013. RACK1 function in cell motility and protein synthesis. Genes Cancer 4:369–377. http://dx.doi.org/10.1177/1947601913486348.
   PubMedGoogle Scholar
• Regmi S, Rothberg KG, Hubbard JG, Ruben L. 2008. The RACK1 signal anchor protein from Trypanosoma brucei associates with eukaryotic elongation factor 1A: a role for translational control in cytokinesis. Mol. Microbiol. 70:724–745. http://dx.doi.org/10.1111/j.1365-2958.2008.06443.x.
   PubMedGoogle Scholar