The elongation, termination, and recycling phases of translation in eukaryotes

Cold Spring Harbor Perspectives in Biology

Volumn 4, Issue 7, 2012, Pages 1-16

  Dever, Thomas E ^a   Green, Rachel ^b  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA;

ELONGATION FACTOR;

EUKARYOTIC CELL; METABOLISM; PROTEIN SYNTHESIS; REGULATOR GENE; REVIEW;

EUKARYOTIC CELLS; PEPTIDE ELONGATION FACTORS; PROTEIN BIOSYNTHESIS; TERMINATOR REGIONS, GENETIC;

EID: 84863904349     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a013706     Document Type: Article

References (121)

1. Alkalaeva EZ, Pisarev AV, Frolova LY, Kisselev LL, Pestova TV. 2006. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125: 1125-1136.
2. 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.
3. Anand M, Balar B, Ulloque R, Gross SR, Kinzy TG. 2006. Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A. J Biol Chem 281: 32318-32326.
4. Andersen DS, Leevers SJ. 2007. The essential Drosophila ATP-binding cassette domain protein, pixie, binds the 40 S ribosome in an ATP-dependent manner and is required for translation initiation. J Biol Chem 282: 14752-14760.
5. Andersen CB, Becker T, Blau M, Anand M, Halic M, Balar B, Mielke T, Boesen T, Pedersen JS, Spahn CM, et al. 2006. Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature 443: 663-668.
6. 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.
7. Bailly M, de Crecy-Lagard V. 2010. Predicting the pathway involved in post-translational modification of elongation factor P in a subset of bacterial species. Biol Direct 5: 3.
8. Balagopal V, Parker R. 2011. Stm1 modulates translation after 80S formation in Saccharomyces cerevisiae. RNA 17: 835-842.
9. Barthelme D, Dinkelaker S, Albers SV, Londei P, Ermler U, Tampe R. 2011. Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proc Natl Acad Sci 108: 3228-3233.
10. Becker T, Armache JP, Jarasch A, Anger AM, Villa E, Sieber H, Motaal BA, Mielke T, Berninghausen O, Beckmann R. 2011. Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome. Nat Struct Mol Biol 18: 715-720.
11. Becker T, Franckenberg S, Wickles S, Shoemaker CJ, Anger AM, Armache JP, Sieber H, Ungewickell C, Berninghausen O, Daberkow I, et al. 2012. Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. Nature 482: 501-506.
12. Ben-Shem A, Jenner L, Yusupova G, Yusupov M. 2010. Crystal structure of the eukaryotic ribosome. Science 330: 1203-1209.
13. Ben-Shem A, Garreau de Loubresse N, Melnikov S, Jenner L, Yusupova G, Yusupov M. 2011. The structure of the eukaryotic ribosome at 3. 0 A resolution. Science 334: 1524-1529.
14. Bernstein P, Peltz SW, Ross J. 1989. The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro. Mol Cell Biol 9: 659-670.
15. Blaha G, Stanley RE, Steitz TA. 2009. Formation of the first peptide bond: The structure of EF-P bound to the 70S ribosome. Science 325: 966-970.
16. Bulygin KN, Khairulina YS, Kolosov PM, Ven'yaminova AG, Graifer DM, Vorobjev YN, Frolova LY, Kisselev LL, Karpova GG. 2010. Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome. RNA 16: 1902-1914.
17. Carlberg U, Nilsson A, Nygard O. 1990. Functional properties of phosphorylated elongation factor 2. Eur J Biochem 191: 639-645.
18. Chavatte L, Seit-Nebi A, Dubovaya V, Favre A. 2002. The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. EMBOJ 21: 5302-5311.
19. Chen CM, Behringer RR. 2004. Ovca1 regulates cell proliferation, embryonic development, and tumorigenesis. Genes Dev 18: 320-332.
20. Chen ZQ, Dong J, Ishimura A, Daar I, Hinnebusch AG, Dean M. 2006. The essential vertebrate ABCE1 protein interacts with eukaryotic initiation factors. J Biol Chem 281: 7452-7457.
21. Chen L, Muhlrad D, Hauryliuk V, Cheng Z, Lim MK, Shyp V, Parker R, Song H. 2010. Structure of the Dom34-Hbs1 complex and implications for no-go decay. Nat Struct Mol Biol 17: 1233-1240.
22. Chen C, Stevens B, Kaur J, Smilansky Z, Cooperman BS, Goldman YE. 2011. Allosteric vs. spontaneous exit-site (E-site) tRNAdissociation early in protein synthesis. Proc Natl Acad Sci 108: 16980-16985.
23. Cheng Z, Saito K, Pisarev AV, Wada M, Pisareva VP, Pestova TV, Gajda M, Round A, Kong C, Lim M, et al. 2009. Structural insights into eRF3 and stop codon recognition by eRF1. Genes Dev 23: 1106-1118.
24. Cosson B, Couturier A, Chabelskaya S, Kiktev D, Inge-Vechtomov S, Philippe M, Zhouravleva G. 2002. Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI{thorn}] propagation. Mol Cell Biol 22: 3301-3315.
25. Dean M, Annilo T. 2005. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Ann Rev Genomics Hum Genet 6: 123-142.
26. Dias CA, Gregio AP, Rossi D, Galvao FC, Watanabe TF, Park MH, Valentini SR, Zanelli CF. 2012. eIF5A interacts functionally with eEF2. Amino Acids 42: 697-702.
27. Dmitriev SE, Terenin IM, Andreev DE, Ivanov PA, Dunaevsky JE, Merrick WC, Shatsky IN. 2010. GTP-independent tRNA delivery to the ribosomal P-site by a novel eukaryotic translation factor. J Biol Chem 285: 26779-26787.
28. Doma MK, Parker R. 2006. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 440: 561-564.
29. Dong J, Lai R, Nielsen K, Fekete CA, Qiu H, Hinnebusch AG. 2004. The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J Biol Chem 279: 42157-42168.
30. Dunkle JA, Wang L, Feldman MB, Pulk A, Chen VB, Kapral GJ, Noeske J, Richardson JS, Blanchard SC, Cate JH. 2011. Structures of the bacterial ribosome in classical and hybrid states of tRNA binding. Science 332: 981-984.
31. Eyler DE, Green R. 2011. Distinct response of yeast ribosomes to a miscoding event during translation. RNA 17: 925-932.
32. Fan-Minogue H, Du M, Pisarev AV, Kallmeyer AK, Salas-Marco J, Keeling KM, Thompson SR, Pestova TV, Bedwell DM. 2008. Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination. Mol Cell 30: 599-609.
33. Freistroffer DV, Pavlov MY, MacDougall J, Buckingham RH, Ehrenberg M. 1997. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J 16: 4126-4133.
34. Frolova L, Le Goff X, Zhouravleva G, Davydova E, Philippe M, Kisselev L. 1996. Eukaryotic polypeptide chain release factor eRF3 is an eRF1-and ribosome-dependent guanosine triphosphatase. RNA 2: 334-341.
35. Frolova LY, Tsivkovskii RY, Sivolobova GF, Oparina NY, Serpinsky OI, Blinov VM, Tatkov SI, Kisselev LL. 1999. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5: 1014-1020.
36. Gao N, Zavialov AV, Li W, Sengupta J, Valle M, Gursky RP, Ehrenberg M, Frank J. 2005. Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies. Mol Cell 18: 663-674.
37. Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC, Ramakrishnan V. 2009. The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science 326: 694-699.
38. Ghosh S, Ganesan R, Amrani N, Jacobson A. 2010. Translational competence of ribosomes released from a premature termination codon is modulated by NMD factors. RNA 16: 1832-1847.
39. Glick BR, Ganoza MC. 1975. Identification of a soluble protein that stimulates peptide bond synthesis. Proc Natl Acad Sci 72: 4257-4260.
40. Graille M, Chaillet M, van Tilbeurgh H. 2008. Structure of yeast Dom34: A protein related to translation termination factor Erf1 and involved inNo-Go decay. J Biol Chem 283: 7145-7154.
41. Gregio AP, Cano VP, Avaca JS, Valentini SR, Zanelli CF. 2009. eIF5A has a function in the elongation step of translation in yeast. Biochem Biophys Res Commun 380: 785-790.
42. He SL, Green R. 2010. Visualization of codon-dependent conformational rearrangements during translation termination. Nat Struct Mol Biol 17: 465-470.
43. Henderson A, Hershey JW. 2011. Eukaryotic translation initiation factor (eIF) 5A stimulates protein synthesis in Saccharomyces cerevisiae. Proc Natl Acad Sci 108: 6415-6419.
44. Hinnebusch AG, Lorsch JR. 2012. The mechanism of eukaryotic translation initiation: New insights and challenges. Cold Spring Harb Perspect Biol doi: 10. 1101/cshperspect.a011544.
45. Hirokawa G, Nijman RM, Raj VS, Kaji H, Igarashi K, Kaji A. 2005. The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits. RNA 11: 1317-1328.
46. Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T. 1999. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 30-Poly(A) tail of mRNA. Direct association of eRF3/ GSPT with polyadenylate-binding protein. J Biol Chem 274: 16677-16680.
47. Ingolia NT, Ghaemmaghami S, Newman JR, Weissman JS. 2009. Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324: 218-223.
48. Ivanov PV, Gehring NH, Kunz JB, Hentze MW, Kulozik AE. 2008. Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways. EMBO J 27: 736-747.
49. Jacobson A. 1996. Poly(A) metabolism and translation: The closed-looped model. In Translational control (ed. Hershey JWB, Mathews M, Sonenberg N), pp. 505-548. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
50. Jao DL, Chen KY. 2006. Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex. J Cell Biochem 97: 583-598.
51. Jenner L, Demeshkina N, Yusupova G, Yusupov M. 2010. Structural rearrangements of the ribosome at the tRNA proofreading step. Nat Struct Mol Biol 17: 1072-1078.
52. Jin H, Kelley AC, Loakes D, Ramakrishnan V. 2010. Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release. Proc Natl Acad Sci 107: 8593-8598.
53. Kang HA, Hershey JW. 1994. Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J Biol Chem 269: 3934-3940.
54. Keeling KM, Salas-Marco J, Osherovich LZ, Bedwell DM. 2006. Tpa1p is part of an mRNP complex that influences translation termination, mRNAdeadenylation, andmRNA turnover in Saccharomyces cerevisiae. Mol Cell Biol 26: 5237-5248.
55. Kemper WM, Berry KW, Merrick WC. 1976. Purification and properties of rabbit reticulocyte protein synthesis initiation factors M2Bα and M2Bβ. J Biol Chem 251: 5551-5557.
56. Kerr ID. 2004. Sequence analysis of twin ATP binding cassette proteins involved in translational control, antibiotic resistance, and ribonuclease L inhibition. Biochem Biophys Res Commun 315: 166-173.
57. Khoshnevis S, Gross T, Rotte C, Baierlein C, Ficner R, Krebber H. 2010. The iron-sulphur protein RNase L inhibitor functions in translation termination. EMBO Rep 11: 214-219.
58. Kim KK, Hung LW, Yokota H, Kim R, Kim SH. 1998. Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1. 8 A° resolution. Proc Natl Acad Sci 95: 10419-10424.
59. Kimata Y, Kohno K. 1994. Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth. J Biol Chem 269: 13497-13501.
60. Klinge S, Voigts-Hoffmann F, Leibundgut M, Arpagaus S, Ban N. 2011. Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6. Science 334: 941-948.
61. Kobayashi K, Kikuno I, Kuroha K, Saito K, Ito K, Ishitani R, Inada T, Nureki O. 2010. Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1a complex. Proc Natl Acad Sci 107: 17575-17579.
62. Kolosov P, Frolova L, Seit-Nebi A, Dubovaya V, Kononenko A, Oparina N, Justesen J, Efimov A, Kisselev L. 2005. Invariant amino acids essential for decoding function of polypeptide release factor eRF1. Nucleic Acids Res 33: 6418-6425.
63. Kononenko AV, Mitkevich VA, Dubovaya VI, Kolosov PM, Makarov AA, Kisselev LL. 2008. Role of the individual domains of translation termination factor eRF1 in GTP binding to eRF3. Proteins 70: 388-393.
64. Korostelev A, Asahara H, Lancaster L, Laurberg M, Hirschi A, Zhu J, Trakhanov S, Scott WG, Noller HF. 2008. Crystal structure of a translation termination complex formed with release factor RF2. Proc Natl Acad Sci 105: 19684-19689.
65. Kozak M. 1984. Selection of initiation sites by eucaryotic ribosomes: Effect of inserting AUG triplets upstream from the coding sequence for preproinsulin. Nucleic Acids Res 12: 3873-3893.
66. Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF. 2008. Structural basis for translation termination on the 70S ribosome. Nature 454: 852-857.
67. Lee HH, Kim YS, Kim KH, Heo I, Kim SK, Kim O, Kim HK, Yoon JY, Kim HS, Kim do J, et al. 2007. Structural and functional insights into Dom34, a key component of nogo mRNA decay. Mol Cell 27: 938-950.
68. Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH. 2004. Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24: 9487-9497.
69. Liu S, Wiggins JF, Sreenath T, Kulkarni AB, Ward JM, Leppla SH. 2006. Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development. Mol Cell Biol 26: 3835-3841.
70. Merkulova TI, Frolova LY, Lazar M, Camonis J, Kisselev LL. 1999. C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction. FEBS Lett 443: 41-47.
71. Navarre WW, Zou SB, Roy H, Xie JL, Savchenko A, Singer A, Edvokimova E, Prost LR, Kumar R, Ibba M, et al. 2010. PoxA, yjeK, and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica. Mol Cell 39: 209-221.
72. Nierhaus KH. 1990. The allosteric three-site model for the ribosomal elongation cycle: Features and future. Biochemistry 29: 4997-5008.
73. Ogle JM, Brodersen DE, Clemons WM Jr, Tarry MJ, Carter AP, Ramakrishnan V. 2001. Recognition of cognate transfer RNA by the 30S ribosomal subunit. Science 292: 897-902.
74. Ortiz PA, Ulloque R, Kihara GK, Zheng H, Kinzy TG. 2006. Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance. J Biol Chem 281: 32639-32648.
75. Pape T, Wintermeyer W, Rodnina MV. 1998. Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J 17: 7490-7497.
76. Park MH, Wolff EC, Smit-McBride Z, Hershey JW, Folk JE. 1991. Comparison of the activities of variant forms of eIF-4D. The requirement for hypusine or deoxyhypusine. J Biol Chem 266: 7988-7994.
77. Park S, Park JM, Kim S, Kim JA, Shepherd JD, Smith-Hicks CL, Chowdhury S, Kaufmann W, Kuhl D, Ryazanov AG, et al. 2008. Elongation factor 2 and fragile X mental retardation protein control the dynamic translation of Arc/ Arg3. 1 essential for mGluR-LTD. Neuron 59: 70-83.
78. Park MH, Nishimura K, Zanelli CF, Valentini SR. 2010. Functional significance of eIF5A and its hypusine modification in eukaryotes. Amino Acids 38: 491-500.
79. Park EH, Zhang F, Warringer J, Sunnerhagen P, Hinnebusch AG. 2011. Depletion of eIF4G fromyeast cells narrows the range of translational efficiencies genome-wide. BMC Genomics 12: 1-18.
80. Park JH, Johansson HE, Aoki H, Huang B, Kim HY, Ganoza MC, Park MH. 2012. Post-translational modification by b-lysylation is required for the activity of E. coli elongation factor P (EF-P). J Biol Chem 287: 2579-2590.
81. Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. 1996. Propagation of the yeast prion-like [psi{thorn}] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 15: 3127-3134.
82. Peske F, Rodnina MV, Wintermeyer W. 2005. Sequence of steps in ribosome recycling as defined by kinetic analysis. Mol Cell 18: 403-412.
83. Pisarev AV, Hellen CU, Pestova TV. 2007. Recycling of eukaryotic posttermination ribosomal complexes. Cell 131: 286-299.
84. Pisarev AV, Skabkin MA, Pisareva VP, Skabkina OV, Rakotondrafara AM, Hentze MW, Hellen CU, Pestova TV. 2010. The role of ABCE1 in eukaryotic posttermination ribosomal recycling. Mol Cell 37: 196-210.
85. Pisareva VP, Pisarev AV, Hellen CU, Rodnina MV, Pestova TV. 2006. Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides. J Biol Chem 281: 40224-40235.
86. Pisareva VP, Skabkin MA, Hellen CU, Pestova TV, Pisarev AV. 2011. Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes. EMBO J 30: 1804-1817.
87. Rodnina MV, Wintermeyer W. 2009. Recent mechanistic insights into eukaryotic ribosomes. Curr Opin Cell Biol 21: 435-443.
88. Sachs AB, Davis RW. 1989. The Poly(A) binding protein is required for Poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell 58: 857-867.
89. Saini P, Eyler DE, Green R, Dever TE. 2009. Hypusine-containing protein eIF5A promotes translation elongation. Nature 459: 118-121.
90. Saito K, Kobayashi K, Wada M, Kikuno I, Takusagawa A, Mochizuki M, Uchiumi T, Ishitani R, Nureki O, Ito K. 2010. Omnipotent role of archaeal elongation factor 1a (EF1a) in translational elongation and termination, and quality control of protein synthesis. Proc Natl Acad Sci 107: 19242-19247.
91. Salas-Marco J, Bedwell DM. 2005. Discrimination between defects in elongation fidelity and termination efficiency provides mechanistic insights into translational readthrough. J Mol Biol 348: 801-815.
92. Schmeing TM, Voorhees RM, Kelley AC, Gao YG, Murphy FVt, Weir JR, Ramakrishnan V. 2009. The crystal structure of the ribosome bound to EF-Tu and aminoacyltRNA. Science 326: 688-694.
93. Schmeing TM, Voorhees RM, Kelley AC, Ramakrishnan V. 2011. How mutations in tRNA distant from the anticodon affect the fidelity of decoding. Nat Struct Mol Biol 18: 432-436.
94. Schreier MH, Erni B, Staehelin T. 1977. Initiation of mammalian protein synthesis: Purification and characterization of seven initiation factors. J Mol Biol 116: 727-753.
95. Semenkov YP, Rodnina MV, Wintermeyer W. 1996. The "allosteric three-site model" of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli. Proc Natl Acad Sci 93: 12183-12188.
96. Shoemaker CJ, Green R. 2011. Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc Natl Acad Sci 108: E1392-E1398.
97. 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.
98. Sivan G, Aviner R, Elroy-Stein O. 2011. Mitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes. J Biol Chem 286: 27927-27935.
99. Skabkin MA, Skabkina OV, Dhote V, Komar AA, Hellen CU, Pestova TV. 2010. Activities of Ligatin and MCT-1/ DENR in eukaryotic translation initiation and ribosomal recycling. Genes Dev 24: 1787-1801.
100. Skogerson L, Engelhardt D. 1977. Dissimilarity in protein chain elongation factor requirements between yeast and rat liver ribosomes. J Biol Chem 252: 1471-1475.
101. Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D. 2000. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100: 311-321.
102. Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski AI, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite MF. 1995. The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14: 4365-4373.
103. Tarun SZ, Sachs AB. 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J 15: 7168-7177.
104. Tarun SZ, Wells SE, Deardorff JA, Sachs AB. 1997. Translation initiation factor eIF4G mediates in vitro poly (A) tail-dependent translation. Proc Natl Acad Sci 94: 9046-9051.
105. Ter-Avanesyan MD, Kushnirov VV, Dagkesamanskaya AR, Didichenko SA, Chernoff YO, Inge-Vechtomov SG, Smirnov VN. 1993. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol 7: 683-692.
106. Triana-Alonso FJ, Chakraburtty K, Nierhaus KH. 1995. The elongation factor unique in higher fungi and essential for protein biosynthesis is an E site factor. J Biol Chem 270: 20473-20478.
107. Uemura S, Aitken CE, Korlach J, Flusberg BA, Turner SW, Puglisi JD. 2010. Real-time tRNA transit on single translating ribosomes at codon resolution. Nature 464: 1012-1017.
108. Van Dyke N, Pickering BF, Van Dyke MW. 2009. Stm1p alters the ribosome association of eukaryotic elongation factor 3 and affects translation elongation. Nucleic Acids Res 37: 6116-6125.
109. Voorhees RM, Schmeing TM, Kelley AC, Ramakrishnan V. 2010. The mechanismfor activation of GTP hydrolysis on the ribosome. Science 330: 835-838.
110. Walden WE, Thach RE. 1986. Translational control of gene expression in a normal fibroblast. Characterization of a subclass of mRNAs with unusual kinetic properties. Biochemistry 25: 2033-2041.
111. Waung MW, Pfeiffer BE, Nosyreva ED, Ronesi JA, Huber KM. 2008. Rapid translation of Arc/Arg3. 1 selectively mediates mGluR-dependent LTD through persistent increases in AMPAR endocytosis rate. Neuron 59: 84-97.
112. Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ. 2008. Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development. J Cell Sci 121: 3140-3145.
113. Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V. 2008. Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322: 953-956.
114. Yanagisawa T, Sumida T, Ishii R, Takemoto C, Yokoyama S. 2010. A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P. Nat Struct Mol Biol 17: 1136-1143.
115. Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC. 2005. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J 24: 580-588.
116. Youngman EM, He SL, Nikstad LJ, Green R. 2007. Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release. Mol Cell 28: 533-543.
117. Zaher HS, Green R. 2011. A primary role for release factor 3 in quality control during translation elongation in Escherichia coli. Cell 147: 396-408.
118. Zanelli CF, Maragno AL, Gregio AP, Komili S, Pandolfi JR, Mestriner CA, Lustri WR, Valentini SR. 2006. eIF5A binds to translational machinery components and affects translation in yeast. Biochem Biophys Res Commun 348: 1358-1366.
119. Zavialov AV, Hauryliuk VV, Ehrenberg M. 2005. Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G. Mol Cell 18: 675-686.
120. Zhao Z, Fang LL, Johnsen R, Baillie DL. 2004. ATP-binding cassette protein E is involved in gene transcription and translation in Caenorhabditis elegans. Biochem Biophys Res Commun 323: 104-111.
121. Zhouravleva G, Frolova L, Le Goff X, Le Guellec R, Inge-Vechtomov S, Kisselev L, Philippe M. 1995. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J 14: 4065-4072.