메뉴 건너뛰기




Volumn 25, Issue 12, 2003, Pages 1201-1211

Starting the protein synthesis machine: Eukaryotic translation initiation

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEIN; PROTEOME; TRANSCRIPTOME; UNCLASSIFIED DRUG;

EID: 0344758983     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.10362     Document Type: Review
Times cited : (159)

References (99)
  • 2
    • 0037133957 scopus 로고    scopus 로고
    • Structure and function of the eukaryotic ribosome:the next frontier
    • Doudna JA, Rath VL. Structure and function of the eukaryotic ribosome: the next frontier. Cell 2002;109:15315-15316.
    • (2002) Cell , vol.109 , pp. 15315-15316
    • Doudna, J.A.1    Rath, V.L.2
  • 3
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan V. Ribosome structure and the mechanism of translation. Cell 2002;108:557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 4
    • 0035371080 scopus 로고    scopus 로고
    • Diversity in translational regulation
    • Macdonald P. Diversity in translational regulation. Curr Opin Cell Biol 2001;13:326-331.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 326-331
    • Macdonald, P.1
  • 5
    • 0036440779 scopus 로고    scopus 로고
    • Regulation of mammalian translation factors by nutrients
    • Proud CG. Regulation of mammalian translation factors by nutrients. Eur J Biochem 2002;269:5338-5349.
    • (2002) Eur J Biochem , vol.269 , pp. 5338-5349
    • Proud, C.G.1
  • 6
    • 0036779335 scopus 로고    scopus 로고
    • Regulation of translational initiation in plants
    • Kawaguchi R, Bailey-Serres J. Regulation of translational initiation in plants. Curr Opin Plant Biol 2002;5:460-465.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 460-465
    • Kawaguchi, R.1    Bailey-Serres, J.2
  • 7
    • 0036797563 scopus 로고    scopus 로고
    • Control of eukaryotic protein synthesis by upstream open reading frames in the 5′-untranslated region of an mRNA
    • Meijer HA, Thomas AA. Control of eukaryotic protein synthesis by upstream open reading frames in the 5′-untranslated region of an mRNA. Biochem J 2002;367:1-11.
    • (2002) Biochem J , vol.367 , pp. 1-11
    • Meijer, H.A.1    Thomas, A.A.2
  • 8
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever TE. Gene-specific regulation by general translation factors. Cell 2002;108:545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 9
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen CU, Sarnow P. Internal ribosome entry sites in eukaryotic mRNA molecules. Genes Dev 2001;15:1593-1612.
    • (2001) Genes Dev , vol.15 , pp. 1593-1612
    • Hellen, C.U.1    Sarnow, P.2
  • 10
    • 0034764497 scopus 로고    scopus 로고
    • Irresistible IRES. Attracting the translation machinery to internal ribosome entry sites
    • Vagner S, Galy B, Pyronnet S. Irresistible IRES. Attracting the translation machinery to internal ribosome entry sites. EMBO Rep 2001;2:893-898.
    • (2001) EMBO Rep , vol.2 , pp. 893-898
    • Vagner, S.1    Galy, B.2    Pyronnet, S.3
  • 11
    • 0035253411 scopus 로고    scopus 로고
    • Cell-cycle-dependent translational control
    • Pyronnet S, Sonenberg N. Cell-cycle-dependent translational control. Curr Opin Genet Dev 2001;11:13-18.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 13-18
    • Pyronnet, S.1    Sonenberg, N.2
  • 12
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras A-C, Raught B, Sonenberg N. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem 1999;68:913-963.
    • (1999) Annu Rev Biochem , vol.68 , pp. 913-963
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 14
    • 0034100762 scopus 로고    scopus 로고
    • Eukaryotic translation initiation: There are (at least) two sides to every story
    • Sachs AB, Varani G. Eukaryotic translation initiation: there are (at least) two sides to every story. Nat Struct Biol 2000;7;356-361.
    • (2000) Nat Struct Biol , vol.7 , pp. 356-361
    • Sachs, A.B.1    Varani, G.2
  • 16
    • 0037121050 scopus 로고    scopus 로고
    • Pushing the limits of the scanning mechanism for initiation of translation
    • Kozak M. Pushing the limits of the scanning mechanism for initiation of translation. Gene 2002;299:1-34.
    • (2002) Gene , vol.299 , pp. 1-34
    • Kozak, M.1
  • 17
    • 0032931764 scopus 로고    scopus 로고
    • The beta subunit of eukaryotic translation initiation factor 2 binds mRNA through the lysine repeats and a region comprising the C2-C2 motif
    • Laurino JP, Thompson GM, Pacheco E, Castilho BA. The beta subunit of eukaryotic translation initiation factor 2 binds mRNA through the lysine repeats and a region comprising the C2-C2 motif. Mol Cell Biol 1999;19:173-181.
    • (1999) Mol Cell Biol , vol.19 , pp. 173-181
    • Laurino, J.P.1    Thompson, G.M.2    Pacheco, E.3    Castilho, B.A.4
  • 18
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano K, Krishnamoorthy T, Phan L, Pavitt GD, Hinnebusch AG. Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J 1999;18:1673-1688.
    • (1999) EMBO J , vol.18 , pp. 1673-1688
    • Asano, K.1    Krishnamoorthy, T.2    Phan, L.3    Pavitt, G.D.4    Hinnebusch, A.G.5
  • 19
    • 0032519585 scopus 로고    scopus 로고
    • eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • Pavitt GD, Ramaiah KV, Kimball SR, Hinnebusch AG. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev 1998;12:514-526.
    • (1998) Genes Dev , vol.12 , pp. 514-526
    • Pavitt, G.D.1    Ramaiah, K.V.2    Kimball, S.R.3    Hinnebusch, A.G.4
  • 20
    • 0031876171 scopus 로고    scopus 로고
    • Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
    • Phan L, Zhang X, Asano K, Anderson J, Vornlocher HP, Greenberg JR, Qin J, Hinnebusch AG. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol Cell Biol 1998;18:4935-4946.
    • (1998) Mol Cell Biol , vol.18 , pp. 4935-4946
    • Phan, L.1    Zhang, X.2    Asano, K.3    Anderson, J.4    Vornlocher, H.P.5    Greenberg, J.R.6    Qin, J.7    Hinnebusch, A.G.8
  • 22
    • 0034307347 scopus 로고    scopus 로고
    • A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo
    • Asano K, Clayton J, Shalev A, Hinnebusch AG. A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo. Genes Dev 2000;14:2534-2546.
    • (2000) Genes Dev , vol.14 , pp. 2534-2546
    • Asano, K.1    Clayton, J.2    Shalev, A.3    Hinnebusch, A.G.4
  • 23
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a. NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
    • Valasek L, Mathew A, Shin BS, Nielsen KH, Szamecz B, Hinnebusch AG. The yeast eIF3 subunits TIF32/a. NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev 2003;17:786-799.
    • (2003) Genes Dev , vol.17 , pp. 786-799
    • Valasek, L.1    Mathew, A.2    Shin, B.S.3    Nielsen, K.H.4    Szamecz, B.5    Hinnebusch, A.G.6
  • 24
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases
    • Lamphear BJ, Kirchweger R, Skern T, Rhoads RE. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. J Biol Chem 1995;270:21975-21983.
    • (1995) J Biol Chem , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 25
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano K, Shalev A, Phan L, Nielsen K, Clayton J, Valassek L, Donahue TF, Hinnebusch AG. Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J 2001;20:2326-2337.
    • (2001) EMBO J , vol.20 , pp. 2326-2337
    • Asano, K.1    Shalev, A.2    Phan, L.3    Nielsen, K.4    Clayton, J.5    Valassek, L.6    Donahue, T.F.7    Hinnebusch, A.G.8
  • 26
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3
    • Methot N, Song MS, Sonenberg N. A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol Cell Biol 1996;16:5328-5334.
    • (1996) Mol Cell Biol , vol.16 , pp. 5328-5334
    • Methot, N.1    Song, M.S.2    Sonenberg, N.3
  • 27
    • 0031439105 scopus 로고    scopus 로고
    • Heat shock increases the association of binding protein-1 with initiation factor 4E
    • Vries RG, Flynn A, Patel JC, Wang X, Denton RM, Proud CG. Heat shock increases the association of binding protein-1 with initiation factor 4E. J Biol Chem 1997;272:32779-32784.
    • (1997) J Biol Chem , vol.272 , pp. 32779-32784
    • Vries, R.G.1    Flynn, A.2    Patel, J.C.3    Wang, X.4    Denton, R.M.5    Proud, C.G.6
  • 28
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 1997;89:951-961.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 30
    • 0037086471 scopus 로고    scopus 로고
    • Crystal structures of 7-methylguanosine 5′-triphosphate (m(7)GTP)-and P(1)-7-methylguanosine-P(3)-adenosine-5′,5′ -triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E:biological importance of the C-terminal flexible region
    • Tomoo K, et al. Crystal structures of 7-methylguanosine 5′-triphosphate (m(7)GTP)-and P(1)-7-methylguanosine-P(3)-adenosine-5′,5′-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E:biological importance of the C-terminal flexible region. Biochem J 2002;362:539-544.
    • (2002) Biochem J , vol.362 , pp. 539-544
    • Tomoo, K.1
  • 31
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers JM, Johnson ER, McKay DB. Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci USA 2000;97:13080-13085.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 32
    • 0028197298 scopus 로고
    • Dominant negative mutants of mammalian eIF-4A define a critical role for eIF-4F in cap-dependent initiation of translation
    • Pause A, Methot N, Svitkin Y, Merrick WC, Sonenberg N. Dominant negative mutants of mammalian eIF-4A define a critical role for eIF-4F in cap-dependent initiation of translation. EMBO J 1994;13:1205-1215.
    • (1994) EMBO J , vol.13 , pp. 1205-1215
    • Pause, A.1    Methot, N.2    Svitkin, Y.3    Merrick, W.C.4    Sonenberg, N.5
  • 33
    • 0035035207 scopus 로고    scopus 로고
    • Tethered-function analysis reveals that eIF4E recruits ribosomes independent of its binding to the cap structure
    • De Gregorio E, Baron J, Preiss T, Hentze MW. Tethered-function analysis reveals that eIF4E recruits ribosomes independent of its binding to the cap structure. RNA 2001;7:106-113.
    • (2001) RNA , vol.7 , pp. 106-113
    • De Gregorio, E.1    Baron, J.2    Preiss, T.3    Hentze, M.W.4
  • 34
    • 0032571398 scopus 로고    scopus 로고
    • Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H
    • Richter-Cook NJ, Dever TE, Hensold JO, Merrick WC. Purification and characterization of a new eukaryotic protein translation factor. Eukaryotic initiation factor 4H. J Biol Chem 1998;273:7579-7587.
    • (1998) J Biol Chem , vol.273 , pp. 7579-7587
    • Richter-Cook, N.J.1    Dever, T.E.2    Hensold, J.O.3    Merrick, W.C.4
  • 35
    • 0031024024 scopus 로고    scopus 로고
    • eIF4G:a multipurpose ribosome adapter?
    • Hentze MW. eIF4G:a multipurpose ribosome adapter? Science 1997;275:500-501.
    • (1997) Science , vol.275 , pp. 500-501
    • Hentze, M.W.1
  • 36
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol Cell 1999;3:707-716.
    • (1999) Mol Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 37
    • 0033597729 scopus 로고    scopus 로고
    • The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1
    • Hershey PE, McWhirter SM, Gross JD, Wagner G, Alber T, Sachs AB. The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1. J Biol Chem 1999;274:21297-21304.
    • (1999) J Biol Chem , vol.274 , pp. 21297-21304
    • Hershey, P.E.1    McWhirter, S.M.2    Gross, J.D.3    Wagner, G.4    Alber, T.5    Sachs, A.B.6
  • 38
    • 0033828440 scopus 로고    scopus 로고
    • Eukaryote-specific domains in translation initiation factors: Implications for translation regulation and evolution of the translation system
    • Aravind L, Koonin EV. Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system. Genome Res 2000;10:1172-1184.
    • (2000) Genome Res , vol.10 , pp. 1172-1184
    • Aravind, L.1    Koonin, E.V.2
  • 39
    • 0034284394 scopus 로고    scopus 로고
    • Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay
    • Ponting CP. Novel eIF4G domain homologues linking mRNA translation with nonsense-mediated mRNA decay. Trends Biochem Sci 2000;25:423-426.
    • (2000) Trends Biochem Sci , vol.25 , pp. 423-426
    • Ponting, C.P.1
  • 40
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap- dependent translation, and the C-terminal one-third functions as a modulatory region
    • Morino S, Imataka H, Svitkin YV, Pestova TV, Sonenberg N. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap- dependent translation, and the C-terminal one-third functions as a modulatory region. Mol Cell Biol 2000;20:468-477.
    • (2000) Mol Cell Biol , vol.20 , pp. 468-477
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 41
    • 0033200316 scopus 로고    scopus 로고
    • Translation driven by an eIF4G core domain in vivo
    • De Gregorio E, Preiss T, Hentze MW. Translation driven by an eIF4G core domain in vivo. EMBO J 1999;18:4865-4874.
    • (1999) EMBO J , vol.18 , pp. 4865-4874
    • De Gregorio, E.1    Preiss, T.2    Hentze, M.W.3
  • 43
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka H, Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol Cell Biol 1997;17:6940-6947.
    • (1997) Mol Cell Biol , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 45
    • 0035800819 scopus 로고    scopus 로고
    • Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo
    • Li W, Belsham GJ, Proud CG. Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact in a 1:1 ratio in vivo. J Biol Chem 2001;276:29111-29115.
    • (2001) J Biol Chem , vol.276 , pp. 29111-29115
    • Li, W.1    Belsham, G.J.2    Proud, C.G.3
  • 46
    • 0032981328 scopus 로고    scopus 로고
    • Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo
    • Waskiewicz AJ, Johnson JC, Penn B, Mahalingam M, Kimball SR, Cooper JA. Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo. Mol Cell Biol 1999;19:1871-1880.
    • (1999) Mol Cell Biol , vol.19 , pp. 1871-1880
    • Waskiewicz, A.J.1    Johnson, J.C.2    Penn, B.3    Mahalingam, M.4    Kimball, S.R.5    Cooper, J.A.6
  • 47
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E
    • Pyronnet S, Imataka H, Gingras AC, Fukunaga R, Hunter T, Sonenberg N. Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J 1999;18:270-279.
    • (1999) EMBO J , vol.18 , pp. 270-279
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 48
    • 0036438924 scopus 로고    scopus 로고
    • Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation?
    • Scheper GC, Proud CG. Does phosphorylation of the cap-binding protein eIF4E play a role in translation initiation? Eur J Biochem 2002;269:5350-5359.
    • (2002) Eur J Biochem , vol.269 , pp. 5350-5359
    • Scheper, G.C.1    Proud, C.G.2
  • 49
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich WB, Balasta ML, Goss DJ, Rhoads RE. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc Natl Acad Sci USA 1994;91:7668-7672.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 50
    • 0037273418 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E attenuates its interaction with mRNA 5′ cap analogs by electrostatic repulsion:intein-mediated protein ligation strategy to obtain phosphorylated protein
    • Zuberek J, et al. Phosphorylation of eIF4E attenuates its interaction with mRNA 5′ cap analogs by electrostatic repulsion:intein-mediated protein ligation strategy to obtain phosphorylated protein. RNA 2003;9:52-61.
    • (2003) RNA , vol.9 , pp. 52-61
    • Zuberek, J.1
  • 51
    • 0036479313 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA
    • Scheper GC, van Kollenburg B, Hu J, Luo Y, Goss DJ, Proud CG. Phosphorylation of eukaryotic initiation factor 4E markedly reduces its affinity for capped mRNA. J Biol Chem 2002;277:3303-3309.
    • (2002) J Biol Chem , vol.277 , pp. 3303-3309
    • Scheper, G.C.1    Van Kollenburg, B.2    Hu, J.3    Luo, Y.4    Goss, D.J.5    Proud, C.G.6
  • 52
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene 1999;234:187-208.
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 53
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 1986;44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 54
    • 0023660877 scopus 로고
    • At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells
    • Kozak M. At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells. J Mol Biol 1987;196:947-950.
    • (1987) J Mol Biol , vol.196 , pp. 947-950
    • Kozak, M.1
  • 55
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • Pestova TV, Borukhov SI, Hellen CU. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 1998;394:854-859.
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.3
  • 56
    • 0033580851 scopus 로고    scopus 로고
    • Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex
    • Chaudhuri J, Chowdhury D, Maitra U. Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex. J Biol Chem 1999;274:17975-17980.
    • (1999) J Biol Chem , vol.274 , pp. 17975-17980
    • Chaudhuri, J.1    Chowdhury, D.2    Maitra, U.3
  • 57
  • 58
    • 0037439198 scopus 로고    scopus 로고
    • Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
    • Olsen DS, Savner EM, Mathew A, Zhang F, Krishnamoorthy T, Phan L, Hinnebusch AG. Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J 2003;22:193-204.
    • (2003) EMBO J , vol.22 , pp. 193-204
    • Olsen, D.S.1    Savner, E.M.2    Mathew, A.3    Zhang, F.4    Krishnamoorthy, T.5    Phan, L.6    Hinnebusch, A.G.7
  • 59
    • 0033963789 scopus 로고    scopus 로고
    • The eIF1A solution structure reveals a large RNA-binding surface important for scanning function
    • Battiste JL, Pestova TV, Hellen CU, Wagner G. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol Cell 2000;5:109-119.
    • (2000) Mol Cell , vol.5 , pp. 109-119
    • Battiste, J.L.1    Pestova, T.V.2    Hellen, C.U.3    Wagner, G.4
  • 60
    • 0033522507 scopus 로고    scopus 로고
    • Structure and interactions of the translation initiation factor eIF1
    • Fletcher CM, Pestova TV, Hellen CU, Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J 1999;18:2631-2637.
    • (1999) EMBO J , vol.18 , pp. 2631-2637
    • Fletcher, C.M.1    Pestova, T.V.2    Hellen, C.U.3    Wagner, G.4
  • 61
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova TV, Kolupaeva VG. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev 2002;16:2906-2922.
    • (2002) Genes Dev , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 63
    • 0037168583 scopus 로고    scopus 로고
    • Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation
    • Lee JH, Pestova TV, Shin BS, Cao C, Choi SK, Dever TE. Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation. Proc Natl Acad Sci USA 2002;99:16689-16694.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16689-16694
    • Lee, J.H.1    Pestova, T.V.2    Shin, B.S.3    Cao, C.4    Choi, S.K.5    Dever, T.E.6
  • 64
    • 0037184985 scopus 로고    scopus 로고
    • Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
    • Shin BS, Maag D, Roll-Mecak A, Arefin MS, Burley SK, Lorsch JR, Dever TE. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell 2002;111:1015-1025.
    • (2002) Cell , vol.111 , pp. 1015-1025
    • Shin, B.S.1    Maag, D.2    Roll-Mecak, A.3    Arefin, M.S.4    Burley, S.K.5    Lorsch, J.R.6    Dever, T.E.7
  • 65
    • 0034703718 scopus 로고    scopus 로고
    • X-Ray structures of the universal translation initiation factor IF2/eIF5B:conformational changes on GDP and GTP binding
    • Roll-Mecak A, Cao C, Dever TE, Burley SK. X-Ray structures of the universal translation initiation factor IF2/eIF5B:conformational changes on GDP and GTP binding. Cell 2000;103:781-792.
    • (2000) Cell , vol.103 , pp. 781-792
    • Roll-Mecak, A.1    Cao, C.2    Dever, T.E.3    Burley, S.K.4
  • 66
    • 0002799007 scopus 로고    scopus 로고
    • Poly(A) metabolism and translation:the closed-loop model
    • Hershey JWB, Mathews MB, Sonenberg N, editors. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Jacobson A. Poly(A) metabolism and translation:the closed-loop model. In: Hershey JWB, Mathews MB, Sonenberg N, editors. Translational control. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press; 1996. p 451-480.
    • (1996) Translational Control , pp. 451-480
    • Jacobson, A.1
  • 67
    • 0025302185 scopus 로고
    • In the beginning is the end: Regulation of poly(A) addition and removal during early development
    • Wickens M. In the beginning is the end: regulation of poly(A) addition and removal during early development. Trends Biochem Sci 1990;15:320-324.
    • (1990) Trends Biochem Sci , vol.15 , pp. 320-324
    • Wickens, M.1
  • 68
    • 0026038913 scopus 로고
    • The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie DR. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev 1991;5:2108-2116.
    • (1991) Genes Dev , vol.5 , pp. 2108-2116
    • Gallie, D.R.1
  • 69
    • 0028034493 scopus 로고
    • Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae
    • Iizuka N, Naiita 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;14:7322-7330.
    • (1994) Mol Cell Biol , vol.14 , pp. 7322-7330
    • Iizuka, N.1    Naiita, L.2    Franzusoff, A.3    Sarnow, P.4
  • 70
    • 0033229825 scopus 로고    scopus 로고
    • Translational control of dosage compensation in Drosophila by Sex-lethal:cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail
    • Gebauer F, Corona DF, Preiss T, Becker PB, Hentze MW. Translational control of dosage compensation in Drosophila by Sex-lethal:cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail. EMBO J 1999;18:6146-6154.
    • (1999) EMBO J , vol.18 , pp. 6146-6154
    • Gebauer, F.1    Corona, D.F.2    Preiss, T.3    Becker, P.B.4    Hentze, M.W.5
  • 71
    • 0034644749 scopus 로고    scopus 로고
    • Cap-poly(A) synergy in mammalian cell-free extracts:Investigation of the requirements for poly(A)-mediated stimulation of translation initiation
    • Michel YM, Poncet D, Piron M, Kean KM, Borman AM. Cap-poly(A) synergy in mammalian cell-free extracts:Investigation of the requirements for poly(A)-mediated stimulation of translation initiation. J Biol Chem 2000;275:32268-32276.
    • (2000) J Biol Chem , vol.275 , pp. 32268-32276
    • Michel, Y.M.1    Poncet, D.2    Piron, M.3    Kean, K.M.4    Borman, A.M.5
  • 72
    • 0034543678 scopus 로고    scopus 로고
    • Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system
    • Bergamini G, Preiss T, Hentze MW. Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system. RNA 2000;6:1781-1790.
    • (2000) RNA , vol.6 , pp. 1781-1790
    • Bergamini, G.1    Preiss, T.2    Hentze, M.W.3
  • 73
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun SZ, Jr, Sachs AB. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev 1995;9:2997-3007.
    • (1995) Genes Dev , vol.9 , pp. 2997-3007
    • Tarun Jr., S.Z.1    Sachs, A.B.2
  • 74
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G
    • Tarun SZ, Jr, Sachs AB. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J 1996;15:7168-7177.
    • (1996) EMBO J , vol.15 , pp. 7168-7177
    • Tarun Jr., S.Z.1    Sachs, A.B.2
  • 75
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation
    • Tarun SZ, Jr, Wells SE, Deardorff JA, Sachs AB. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc Nat Acad Sci USA 1997;94:9046-9051.
    • (1997) Proc Nat Acad Sci USA , vol.94 , pp. 9046-9051
    • Tarun Jr., S.Z.1    Wells, S.E.2    Deardorff, J.A.3    Sachs, A.B.4
  • 76
    • 0034327417 scopus 로고    scopus 로고
    • Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates:the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′-end
    • Borman AM, Michel YM, Kean KM. Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates:the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′-end. Nucleic Acids Res 2000;28:4068-4075.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4068-4075
    • Borman, A.M.1    Michel, Y.M.2    Kean, K.M.3
  • 77
    • 0037184089 scopus 로고    scopus 로고
    • Free poly(A) stimulates capped mRNA translation in vitro through the eIF4G-poly(A)-binding protein interaction
    • Borman AM, Michel YM, Malnou CE, Kean KM. Free poly(A) stimulates capped mRNA translation in vitro through the eIF4G-poly(A)-binding protein interaction. J Biol Chem 2002;277:36818-36824.
    • (2002) J Biol Chem , vol.277 , pp. 36818-36824
    • Borman, A.M.1    Michel, Y.M.2    Malnou, C.E.3    Kean, K.M.4
  • 78
    • 0345216954 scopus 로고    scopus 로고
    • The end in sight:poly(A), translation and mRNA stability in eukaryotes
    • Brakier-Gingras L, Lapointe J, editors. Georgetown, Texas: Landes Bioscience
    • Preiss T. The end in sight:poly(A), translation and mRNA stability in eukaryotes. In: Brakier-Gingras L, Lapointe J, editors. Translation Mechanisms. Georgetown, Texas: Landes Bioscience; 2003.
    • (2003) Translation Mechanisms
    • Preiss, T.1
  • 79
    • 0023119755 scopus 로고
    • Circular polysomes predominate on the rough endoplasmic reticulum of somatotropes and mammotropes in the rat anterior pituitary
    • Christensen AK, Kahn LE, Bourne CM. Circular polysomes predominate on the rough endoplasmic reticulum of somatotropes and mammotropes in the rat anterior pituitary. Am J Anat 1987;178:1-10.
    • (1987) Am J Anat , vol.178 , pp. 1-10
    • Christensen, A.K.1    Kahn, L.E.2    Bourne, C.M.3
  • 80
    • 0032473954 scopus 로고    scopus 로고
    • Dual function of the messenger RNA cap structure in poly(A) -tail-promoted translation in yeast
    • Preiss T, Hentze MW. Dual function of the messenger RNA cap structure in poly(A)-tail-promoted translation in yeast. Nature 1998;392:516-520.
    • (1998) Nature , vol.392 , pp. 516-520
    • Preiss, T.1    Hentze, M.W.2
  • 81
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells SE, Hillner PE, Vale RD, Sachs AB. Circularization of mRNA by eukaryotic translation initiation factors. Mol Cell 1998;2:135-140.
    • (1998) Mol Cell , vol.2 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 82
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • Le H, Tanguay RL, Balasta ML, Wei CC, Browning KS, Metz AM, Goss DJ, Gallie DR. Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. J Biol Chem 1997;272:16247-16255.
    • (1997) J Biol Chem , vol.272 , pp. 16247-16255
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.C.4    Browning, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 83
    • 0032190508 scopus 로고    scopus 로고
    • Rotavirus RNA-binding protein NSP3 interacts with eIF4Gl and evicts the poly(A) binding protein from eIF4F
    • Piron M, Vende P, Cohen J, Poncet D. Rotavirus RNA-binding protein NSP3 interacts with eIF4Gl and evicts the poly(A) binding protein from eIF4F. EMBO J 1998;17:5811-5821.
    • (1998) EMBO J , vol.17 , pp. 5811-5821
    • Piron, M.1    Vende, P.2    Cohen, J.3    Poncet, D.4
  • 84
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataka H, Gradi A, Sonenberg N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J 1998;17:7480-7489.
    • (1998) EMBO J , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 85
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
    • Craig AWB, Haghighat A, Yu ATK, Sonenberg N. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 1998;392:520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.B.1    Haghighat, A.2    Yu, A.T.K.3    Sonenberg, N.4
  • 89
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo RC, Bonanno JB, Sonenberg N, Burley SK. Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell 1999;98:835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 90
    • 0031972645 scopus 로고    scopus 로고
    • RNA recognition motif 2 of yeast Pab 1p is required for its functional interaction with eukaryotic translation initiation factor 4G
    • Kessler SH, Sachs AB. RNA recognition motif 2 of yeast Pab 1p is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol Cell Biol 1998;18:51-57.
    • (1998) Mol Cell Biol , vol.18 , pp. 51-57
    • Kessler, S.H.1    Sachs, A.B.2
  • 91
    • 0033153302 scopus 로고    scopus 로고
    • The yeast poly(A)-binding protein Pab 1p stimulates in vitro poly(A)- dependent and cap-dependent translation by distinct mechanisms
    • Otero LJ, Ashe MP, Sachs AB. The yeast poly(A)-binding protein Pab 1p stimulates in vitro poly(A)- dependent and cap-dependent translation by distinct mechanisms. EMBO J 1999;18:3153-3163.
    • (1999) EMBO J , vol.18 , pp. 3153-3163
    • Otero, L.J.1    Ashe, M.P.2    Sachs, A.B.3
  • 93
    • 0035836636 scopus 로고    scopus 로고
    • X-ray structure of the human hyperplastic discs protein:an ortholog of the C-terminal domain of poly(A)-binding protein
    • Deo RC, Sonenberg N, Burley SK. X-ray structure of the human hyperplastic discs protein:an ortholog of the C-terminal domain of poly(A)-binding protein. Proc Natl Acad Sci USA 2001;98:4414-4419.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4414-4419
    • Deo, R.C.1    Sonenberg, N.2    Burley, S.K.3
  • 94
    • 0037184899 scopus 로고    scopus 로고
    • A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in Cap/Poly(A)-dependent translation
    • Uchida N, Hoshino S, Imataka H, Sonenberg N, Katada T. A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in Cap/Poly(A)-dependent translation. J Biol Chem 2002;277:50286-50292.
    • (2002) J Biol Chem , vol.277 , pp. 50286-50292
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 95
    • 1842403614 scopus 로고    scopus 로고
    • Binding of eukaryotic translation initiation factor 4E (eIF4E) to eIF4G represses translation of uncapped mRNA
    • Tarun SZ, Jr, Sachs AB. Binding of eukaryotic translation initiation factor 4E (eIF4E) to eIF4G represses translation of uncapped mRNA. Mol Cell Biol 1997;17:6876-6886.
    • (1997) Mol Cell Biol , vol.17 , pp. 6876-6886
    • Tarun Jr., S.Z.1    Sachs, A.B.2
  • 96
    • 0030832026 scopus 로고    scopus 로고
    • eIF4G dramatically enhances the binding of eIF4E to the mRNA 5′-cap structure
    • Haghighat A, Sonenberg N. eIF4G dramatically enhances the binding of eIF4E to the mRNA 5′-cap structure. J Biol Chem 1997;272:21677-21680.
    • (1997) J Biol Chem , vol.272 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2
  • 97
    • 0032541425 scopus 로고    scopus 로고
    • Cooperative modulation by eIF4G of eIF4E-binding to the mRNA 5′ cap in yeast involves a site partially shared by p20
    • Ptushkina M, von der Haar T, Vasilescu S, Frank R, Birkenhager R, McCarthy JE. Cooperative modulation by eIF4G of eIF4E-binding to the mRNA 5′ cap in yeast involves a site partially shared by p20. EMBO J 1998;17:4798-4808.
    • (1998) EMBO J , vol.17 , pp. 4798-4808
    • Ptushkina, M.1    Von Der Haar, T.2    Vasilescu, S.3    Frank, R.4    Birkenhager, R.5    McCarthy, J.E.6
  • 98
    • 0033565233 scopus 로고    scopus 로고
    • Repressor binding to a dorsal regulatory site traps human eIF4E in a high cap-affinity state
    • Ptushkina M, von der Haar T, Karim MM, Hughes JMX, McCarthy JE. Repressor binding to a dorsal regulatory site traps human eIF4E in a high cap-affinity state. EMBO J 1999;18:4068-4075.
    • (1999) EMBO J , vol.18 , pp. 4068-4075
    • Ptushkina, M.1    Von Der Haar, T.2    Karim, M.M.3    Hughes, J.M.X.4    McCarthy, J.E.5
  • 99
    • 0032539532 scopus 로고    scopus 로고
    • Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues
    • Wei CC, Balasta ML, Ren J, Goss DJ. Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues. Biochemistry 1998;37:1910-1916.
    • (1998) Biochemistry , vol.37 , pp. 1910-1916
    • Wei, C.C.1    Balasta, M.L.2    Ren, J.3    Goss, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.