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Volumn 19, Issue 6, 2012, Pages 568-576

A mechanistic overview of translation initiation in eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 2ALPHA; INITIATION FACTOR 3; INITIATION FACTOR 4A; INITIATION FACTOR 4B; INITIATION FACTOR 4G; INITIATION FACTOR 5; MESSENGER RNA; TERNARY COMPLEX FACTOR; TRANSFER RNA;

EID: 84861843696     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2303     Document Type: Review
Times cited : (306)

References (108)
  • 1
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg, N. & Hinnebusch, A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136, 731-745 (2009).
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 2
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson, R.J., Hellen, C.U.T. & Pestova, T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11, 113-127 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.T.2    Pestova, T.V.3
  • 3
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • Hinnebusch, A.G. Molecular mechanism of scanning and start codon selection in eukaryotes. Microbiol. Mol. Biol. Rev. 75, 434-467 (2011).
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 4
    • 71549155597 scopus 로고    scopus 로고
    • Eukaryotic initiator tRNA: Finely tuned and ready for action
    • Kolitz, S.E. & Lorsch, J.R. Eukaryotic initiator tRNA: finely tuned and ready for action. FEBS Lett. 584, 396-404 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 396-404
    • Kolitz, S.E.1    Lorsch, J.R.2
  • 5
    • 0347123543 scopus 로고    scopus 로고
    • GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2
    • Kapp, L.D. & Lorsch, J. GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2. J. Mol. Biol. 335, 923-936 (2004).
    • (2004) J. Mol. Biol. , vol.335 , pp. 923-936
    • Kapp, L.D.1    Lorsch, J.2
  • 6
    • 77957676706 scopus 로고    scopus 로고
    • TRNA binding properties of eukaryotic translation initiation factor 2 from Encephalitozoon cuniculi
    • Naveau, M., Lazennec-Schurdevin, C., Panvert, M., Mechulam, Y. & Schmitt, E. tRNA binding properties of eukaryotic translation initiation factor 2 from Encephalitozoon cuniculi. Biochemistry 49, 8680-8688 (2010).
    • (2010) Biochemistry , vol.49 , pp. 8680-8688
    • Naveau, M.1    Lazennec-Schurdevin, C.2    Panvert, M.3    Mechulam, Y.4    Schmitt, E.5
  • 7
    • 80555131009 scopus 로고    scopus 로고
    • Met ternary complex binding to the 40S ribosome
    • Provides the first structural information on the position and architecture of the ternary complex on the 40S subunit
    • Met ternary complex binding to the 40S ribosome. Nat. Struct. Mol. Biol. 18, 1227-1234 (2011). Provides the first structural information on the position and architecture of the ternary complex on the 40S subunit.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1227-1234
    • Shin, B.-S.1
  • 9
    • 3843096103 scopus 로고    scopus 로고
    • Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo
    • Singh, C.R., He, H., Ii, M., Yamamoto, Y. & Asano, K. Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo. J. Biol. Chem. 279, 31910-31920 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 31910-31920
    • Singh, C.R.1    He, H.2    Ii, M.3    Yamamoto, Y.4    Asano, K.5
  • 10
    • 0037439198 scopus 로고    scopus 로고
    • Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
    • Olsen, D.S. et al. Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J. 22, 193-204 (2003).
    • (2003) EMBO J. , vol.22 , pp. 193-204
    • Olsen, D.S.1
  • 11
    • 33644779804 scopus 로고    scopus 로고
    • +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
    • +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev. 20, 624-636 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 624-636
    • Pisarev, A.V.1
  • 12
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano, K. et al. Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J. 20, 2326-2337 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2326-2337
    • Asano, K.1
  • 13
    • 0036224032 scopus 로고    scopus 로고
    • Development and characterization of a reconstituted yeast translation initiation system
    • Algire, M.A. et al. Development and characterization of a reconstituted yeast translation initiation system. RNA 8, 382-397 (2002).
    • (2002) RNA , vol.8 , pp. 382-397
    • Algire, M.A.1
  • 14
    • 0037458626 scopus 로고    scopus 로고
    • Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 40 S preinitiation complex
    • Majumdar, R., Bandyopadhyay, A. & Maitra, U. Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 40 S preinitiation complex. J. Biol. Chem. 278, 6580-6587 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 6580-6587
    • Majumdar, R.1    Bandyopadhyay, A.2    Maitra, U.3
  • 15
    • 10644277580 scopus 로고    scopus 로고
    • Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association
    • Kolupaeva, V.G., Unbehaun, A., Lomakin, I.B., Hellen, C.U.T. & Pestova, T.V. Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association. RNA 11, 470-486 (2005).
    • (2005) RNA , vol.11 , pp. 470-486
    • Kolupaeva, V.G.1    Unbehaun, A.2    Lomakin, I.B.3    Hellen, C.U.T.4    Pestova, T.V.5
  • 16
    • 0345305759 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing
    • Lomakin, I.B. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev. 17, 2786-2797 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 2786-2797
    • Lomakin, I.B.1
  • 17
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Crystal structure of the Tetrahymena 40S subunit bound to eIF1, suggesting a mechanism for eIF1 release upon full accommodation of the initiator tRNA into the P site
    • Rabl, J., Leibundgut, M., Ataide, S.F., Haag, A. & Ban, N. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331, 730-736 (2011). Crystal structure of the Tetrahymena 40S subunit bound to eIF1, suggesting a mechanism for eIF1 release upon full accommodation of the initiator tRNA into the P site.
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 18
    • 69849092725 scopus 로고    scopus 로고
    • Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing
    • Maps the positions of the eIF1A domains on the 40S subunit
    • Yu, Y. et al. Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing. Nucleic Acids Res. 37, 5167-5182 (2009). Maps the positions of the eIF1A domains on the 40S subunit.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5167-5182
    • Yu, Y.1
  • 19
    • 33744957161 scopus 로고    scopus 로고
    • Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2Bε
    • Alone, P.V. & Dever, T.E. Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2Bε. J. Biol. Chem. 281, 12636-12644 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 12636-12644
    • Alone, P.V.1    Dever, T.E.2
  • 20
    • 0035191271 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein
    • Paulin, F.E., Campbell, L.E., O'Brien, K., Loughlin, J. & Proud, C.G. Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein. Curr. Biol. 11, 55-59 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 55-59
    • Paulin, F.E.1    Campbell, L.E.2    O'Brien, K.3    Loughlin, J.4    Proud, C.G.5
  • 21
    • 0035794125 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein
    • Das, S., Ghosh, R. & Maitra, U. Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein. J. Biol. Chem. 276, 6720-6726 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6720-6726
    • Das, S.1    Ghosh, R.2    Maitra, U.3
  • 22
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano, K., Krishnamoorthy, T., Phan, L., Pavitt, G.D. & Hinnebusch, A.G. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18, 1673-1688 (1999).
    • (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
  • 23
    • 28044445673 scopus 로고    scopus 로고
    • The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G
    • Yamamoto, Y. et al. The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G. Proc. Natl. Acad. Sci. USA 102, 16164-16169 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16164-16169
    • Yamamoto, Y.1
  • 24
    • 28544439977 scopus 로고    scopus 로고
    • Structural roles for human translation factor eIF3 in initiation of protein synthesis
    • Siridechadilok, B., Fraser, C., Hall, R. & Doudna, J. Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310, 1513-1515 (2005).
    • (2005) Science , vol.310 , pp. 1513-1515
    • Siridechadilok, B.1    Fraser, C.2    Hall, R.3    Doudna, J.4
  • 25
    • 44649095899 scopus 로고    scopus 로고
    • Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
    • Provides structural information on the relative positions of eIF3 and mRNA on the 40S subunit
    • Pisarev, A.V., Kolupaeva, V.G., Yusupov, M.M., Hellen, C.U.T. & Pestova, T.V. Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes. EMBO J. 27, 1609-1621 (2008). Provides structural information on the relative positions of eIF3 and mRNA on the 40S subunit.
    • (2008) EMBO J. , vol.27 , pp. 1609-1621
    • Pisarev, A.V.1    Kolupaeva, V.G.2    Yusupov, M.M.3    Hellen, C.U.T.4    Pestova, T.V.5
  • 26
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
    • Valášek, L. et al. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev. 17, 786-799 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 786-799
    • Valášek, L.1
  • 27
    • 77956713468 scopus 로고    scopus 로고
    • The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons
    • Chiu, W.-L. et al. The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol. Cell. Biol. 30, 4415-4434 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4415-4434
    • Chiu, W.-L.1
  • 28
    • 84855867417 scopus 로고    scopus 로고
    • The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit
    • Sokabe, M., Fraser, C.S. & Hershey, J.W.B. The human translation initiation multi-factor complex promotes methionyl-tRNAi binding to the 40S ribosomal subunit. Nucleic Acids Res. 40, 905-913 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 905-913
    • Sokabe, M.1    Fraser, C.S.2    Hershey, J.W.B.3
  • 29
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valášek, L., Nielsen, K.H. & Hinnebusch, A.G. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J. 21, 5886-5898 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5886-5898
    • Valášek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 30
    • 1842576663 scopus 로고    scopus 로고
    • Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control
    • Nielsen, K.H. et al. Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control. EMBO J. 23, 1166-1177 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1166-1177
    • Nielsen, K.H.1
  • 31
    • 6344291066 scopus 로고    scopus 로고
    • Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection
    • Valášek, L., Nielsen, K.H., Zhang, F., Fekete, C.A. & Hinnebusch, A.G. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol. Cell. Biol. 24, 9437-9455 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9437-9455
    • Valášek, L.1    Nielsen, K.H.2    Zhang, F.3    Fekete, C.A.4    Hinnebusch, A.G.5
  • 32
    • 20744451862 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation
    • Singh, C.R. et al. Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation. Mol. Cell. Biol. 25, 5480-5491 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5480-5491
    • Singh, C.R.1
  • 33
    • 32044467711 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast
    • Provides evidence for the central role of eIF3 in mRNA recruitment in vivo
    • Jivotovskaya, A.V., Valášek, L., Hinnebusch, A.G. & Nielsen, K.H. Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast. Mol. Cell. Biol. 26, 1355-1372 (2006). Provides evidence for the central role of eIF3 in mRNA recruitment in vivo.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valášek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 34
    • 0242426044 scopus 로고    scopus 로고
    • Rpg1p, the subunit of the Saccharomyces cerevisiae eIF3 core complex, is a microtubule-interacting protein
    • Hasek, J. et al. Rpg1p, the subunit of the Saccharomyces cerevisiae eIF3 core complex, is a microtubule-interacting protein. Cell Motil. Cytoskeleton 45, 235-246 (2000).
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 235-246
    • Hasek, J.1
  • 35
    • 0034801441 scopus 로고    scopus 로고
    • Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p
    • Palecek, J., Hasek, J. & Ruis, H. Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p. Biochem. Biophys. Res. Commun. 282, 1244-1250 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 1244-1250
    • Palecek, J.1    Hasek, J.2    Ruis, H.3
  • 36
    • 0034955565 scopus 로고    scopus 로고
    • Two subcellular localizations of eIF3 p170 and its interaction with membrane-bound microfilaments: Implications for alternative functions of p170
    • Pincheira, R., Chen, Q., Huang, Z. & Zhang, J.T. Two subcellular localizations of eIF3 p170 and its interaction with membrane-bound microfilaments: implications for alternative functions of p170. Eur. J. Cell Biol. 80, 410-418 (2001).
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 410-418
    • Pincheira, R.1    Chen, Q.2    Huang, Z.3    Zhang, J.T.4
  • 37
    • 0037675905 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit
    • Maag, D. Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit. J. Mol. Biol. 330, 917-924 (2003).
    • (2003) J. Mol. Biol. , vol.330 , pp. 917-924
    • Maag, D.1
  • 38
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • Pestova, T.V., Borukhov, S.I. & Hellen, C.U.T. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 394, 854-859 (1998).
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.T.3
  • 39
    • 34047263278 scopus 로고    scopus 로고
    • The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome
    • Cryo-EM reconstructions highlighting the role of eIF1 in stabilizing the open state of the 40S subunit
    • Passmore, L.A. et al. The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol. Cell 26, 41-50 (2007). Cryo-EM reconstructions highlighting the role of eIF1 in stabilizing the open state of the 40S subunit.
    • (2007) Mol. Cell , vol.26 , pp. 41-50
    • Passmore, L.A.1
  • 40
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • Demonstrates that eIF1 is released from the PIC upon start codon recognition
    • Maag, D., Fekete, C., Gryczynski, Z. & Lorsch, J. A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon. Mol. Cell 17, 265-275 (2005). Demonstrates that eIF1 is released from the PIC upon start codon recognition.
    • (2005) Mol. Cell , vol.17 , pp. 265-275
    • Maag, D.1    Fekete, C.2    Gryczynski, Z.3    Lorsch, J.4
  • 41
    • 73549103606 scopus 로고    scopus 로고
    • Met binding to the ribosome
    • Maps the regions of the eIF1A CTT and NTT responsible for their opposing roles in start codon recognition
    • Met binding to the ribosome. Genes Dev. 24, 97-110 (2010). Maps the regions of the eIF1A CTT and NTT responsible for their opposing roles in start codon recognition.
    • (2010) Genes Dev. , vol.24 , pp. 97-110
    • Saini, A.K.1    Nanda, J.S.2    Lorsch, J.R.3    Hinnebusch, A.G.4
  • 42
    • 33947595152 scopus 로고    scopus 로고
    • N- And C-terminal residues of eIF1A have opposing effects on the fidelity of start codon selection
    • Fekete, C.A. et al. N- and C-terminal residues of eIF1A have opposing effects on the fidelity of start codon selection. EMBO J. 26, 1602-1614 (2007).
    • (2007) EMBO J. , vol.26 , pp. 1602-1614
    • Fekete, C.A.1
  • 43
    • 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. 274, 17975-17980 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17975-17980
    • Chaudhuri, J.1    Chowdhury, D.2    Maitra, U.3
  • 44
    • 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.-I., 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. 277, 50286-50292 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 50286-50292
    • Uchida, N.1    Hoshino, S.-I.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 45
    • 78751609906 scopus 로고    scopus 로고
    • Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1•PABP mRNPs in vivo
    • Park, E.-H. et al. Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1•PABP mRNPs in vivo. EMBO J. 30, 302-316 (2011).
    • (2011) EMBO J. , vol.30 , pp. 302-316
    • Park, E.-H.1
  • 46
    • 67650566334 scopus 로고    scopus 로고
    • Intrinsic RNA binding by the eukaryotic initiation factor 4F depends on a minimal RNA length but not on the m7G cap
    • Kaye, N.M., Emmett, K.J., Merrick, W.C. & Jankowsky, E. Intrinsic RNA binding by the eukaryotic initiation factor 4F depends on a minimal RNA length but not on the m7G cap. J. Biol. Chem. 284, 17742-17750 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17742-17750
    • Kaye, N.M.1    Emmett, K.J.2    Merrick, W.C.3    Jankowsky, E.4
  • 47
    • 77956940474 scopus 로고    scopus 로고
    • The 5′-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway
    • Demonstrates that eIF3 is critical for mRNA recruitment in vitro and identifies a new role for the 5′ cap in blocking the formation of aberrant 43S-mRNA complexes
    • Mitchell, S.F. et al. The 5′-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway. Mol. Cell 39, 950-962 (2010). Demonstrates that eIF3 is critical for mRNA recruitment in vitro and identifies a new role for the 5′ cap in blocking the formation of aberrant 43S-mRNA complexes.
    • (2010) Mol. Cell , vol.39 , pp. 950-962
    • Mitchell, S.F.1
  • 48
    • 62849126891 scopus 로고    scopus 로고
    • Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap
    • Yanagiya, A. et al. Requirement of RNA binding of mammalian eukaryotic translation initiation factor 4GI (eIF4GI) for efficient interaction of eIF4E with the mRNA cap. Mol. Cell. Biol. 29, 1661-1669 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1661-1669
    • Yanagiya, A.1
  • 49
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation
    • Tarun, S.Z., Wells, S., Deardorff, J. & Sachs, A. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. USA 94, 9046-9051 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9046-9051
    • Tarun, S.Z.1    Wells, S.2    Deardorff, J.3    Sachs, A.4
  • 50
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • Kahvejian, A., Svitkin, Y.V., Sukarieh, R., M'Boutchou, M.-N. & Sonenberg, N. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev. 19, 104-113 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.-N.4    Sonenberg, N.5
  • 51
    • 33847332134 scopus 로고    scopus 로고
    • Functional analysis of individual binding activities of the scaffold protein eIF4G
    • Hinton, T.M., Coldwell, M.J., Carpenter, G.A., Morley, S.J. & Pain, V.M. Functional analysis of individual binding activities of the scaffold protein eIF4G. J. Biol. Chem. 282, 1695-1708 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 1695-1708
    • Hinton, T.M.1    Coldwell, M.J.2    Carpenter, G.A.3    Morley, S.J.4    Pain, V.M.5
  • 52
    • 58149330117 scopus 로고    scopus 로고
    • General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation
    • Provides evidence that the effects of PABP and the poly(A) tail are most pronounced under conditions of strong competition for mRNA binding
    • Svitkin, Y.V. et al. General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation. EMBO J. 28, 58-68 (2009). Provides evidence that the effects of PABP and the poly(A) tail are most pronounced under conditions of strong competition for mRNA binding.
    • (2009) EMBO J. , vol.28 , pp. 58-68
    • Svitkin, Y.V.1
  • 53
    • 42449138319 scopus 로고    scopus 로고
    • eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy
    • Ramírez-Valle, F., Braunstein, S., Zavadil, J., Formenti, S.C. & Schneider, R.J. eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy. J. Cell Biol. 181, 293-307 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 293-307
    • Ramírez-Valle, F.1    Braunstein, S.2    Zavadil, J.3    Formenti, S.C.4    Schneider, R.J.5
  • 54
    • 79251570260 scopus 로고    scopus 로고
    • Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide
    • Park, E.-H., Zhang, F., Warringer, J., Sunnerhagen, P. & Hinnebusch, A.G. Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide. BMC Genomics 12, 68 (2011).
    • (2011) BMC Genomics , vol.12 , pp. 68
    • Park, E.-H.1    Zhang, F.2    Warringer, J.3    Sunnerhagen, P.4    Hinnebusch, A.G.5
  • 55
    • 68249152550 scopus 로고    scopus 로고
    • Evidence for variation in the optimal translation initiation complex: Plant eIF4B, eIF4F, and eIF(iso)4F differentially promote translation of mRNAs
    • Mayberry, L.K., Allen, M.L., Dennis, M.D. & Browning, K.S. Evidence for variation in the optimal translation initiation complex: plant eIF4B, eIF4F, and eIF(iso)4F differentially promote translation of mRNAs. Plant Physiol. 150, 1844-1854 (2009).
    • (2009) Plant Physiol. , vol.150 , pp. 1844-1854
    • Mayberry, L.K.1    Allen, M.L.2    Dennis, M.D.3    Browning, K.S.4
  • 56
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • Lorsch, J.R. & Herschlag, D. The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry 37, 2180-2193 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 57
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku, T., Nureki, O., Nakamura, A., Kobayashi, S. & Yokoyama, S. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125, 287-300 (2006).
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 58
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu, F., Putnam, A. & Jankowsky, E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc. Natl. Acad. Sci. USA 105, 20209-20214 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 59
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eIF4A helicase activity by eIF4G
    • Oberer, M., Marintchev, A. & Wagner, G. Structural basis for the enhancement of eIF4A helicase activity by eIF4G. Genes Dev. 19, 2212-2223 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 60
    • 59049092956 scopus 로고    scopus 로고
    • Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation
    • Marintchev, A. et al. Topology and regulation of the human eIF4A/4G/4H helicase complex in translation initiation. Cell 136, 447-460 (2009).
    • (2009) Cell , vol.136 , pp. 447-460
    • Marintchev, A.1
  • 61
    • 79953675393 scopus 로고    scopus 로고
    • EIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism
    • Hilbert, M., Kebbel, F., Gubaev, A. & Klostermeier, D. eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucleic Acids Res. 39, 2260-2270 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2260-2270
    • Hilbert, M.1    Kebbel, F.2    Gubaev, A.3    Klostermeier, D.4
  • 62
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F
    • Rogers, G.W., Richter, N.J., Lima, W.F. & Merrick, W.C. Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J. Biol. Chem. 276, 30914-30922 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 30914-30922
    • Rogers, G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 63
    • 52949097997 scopus 로고    scopus 로고
    • Interactions between eIF4AI and its accessory factors eIF4B and eIF4H
    • Rozovsky, N., Butterworth, A.C. & Moore, M.J. Interactions between eIF4AI and its accessory factors eIF4B and eIF4H. RNA 14, 2136-2148 (2008).
    • (2008) RNA , vol.14 , pp. 2136-2148
    • Rozovsky, N.1    Butterworth, A.C.2    Moore, M.J.3
  • 64
    • 0034674029 scopus 로고    scopus 로고
    • Wheat germ translation initiation factor eIF4B affects eIF4A and eIFiso4F helicase activity by increasing the ATP binding affinity of eIF4A
    • Bi, X., Ren, J. & Goss, D.J. Wheat germ translation initiation factor eIF4B affects eIF4A and eIFiso4F helicase activity by increasing the ATP binding affinity of eIF4A. Biochemistry 39, 5758-5765 (2000).
    • (2000) Biochemistry , vol.39 , pp. 5758-5765
    • Bi, X.1    Ren, J.2    Goss, D.J.3
  • 65
    • 61349176586 scopus 로고    scopus 로고
    • Translation initiation factor 4B homodimerization, RNA binding, and interaction with Poly(A)-binding protein are enhanced by zinc
    • Cheng, S., Sultana, S., Goss, D.J. & Gallie, D.R. Translation initiation factor 4B homodimerization, RNA binding, and interaction with Poly(A)-binding protein are enhanced by zinc. J. Biol. Chem. 283, 36140-36153 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 36140-36153
    • Cheng, S.1    Sultana, S.2    Goss, D.J.3    Gallie, D.R.4
  • 66
    • 80052965200 scopus 로고    scopus 로고
    • Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B
    • Özeş, A.R., Feoktistova, K., Avanzino, B.C. & Fraser, C.S. Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. J. Mol. Biol. 412, 674-687 (2011).
    • (2011) J. Mol. Biol. , vol.412 , pp. 674-687
    • Özeş, A.R.1    Feoktistova, K.2    Avanzino, B.C.3    Fraser, C.S.4
  • 67
    • 79954609242 scopus 로고    scopus 로고
    • Synergistic activation of eIF4A by eIF4B and eIF4G
    • Nielsen, K.H. et al. Synergistic activation of eIF4A by eIF4B and eIF4G. Nucleic Acids Res. 39, 2678-2689 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2678-2689
    • Nielsen, K.H.1
  • 68
    • 0029086291 scopus 로고
    • The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity
    • Altmann, M., Wittmer, B., Methot, N., Sonenberg, N. & Trachsel, H. The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity. EMBO J. 14, 3820-3827 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3820-3827
    • Altmann, M.1    Wittmer, B.2    Methot, N.3    Sonenberg, N.4    Trachsel, H.5
  • 69
    • 0031717152 scopus 로고    scopus 로고
    • The RNA recognition motif of yeast translation initiation factor Tif3/eIF4B is required but not sufficient for RNA strand-exchange and translational activity
    • Niederberger, N., Trachsel, H. & Altmann, M. The RNA recognition motif of yeast translation initiation factor Tif3/eIF4B is required but not sufficient for RNA strand-exchange and translational activity. RNA 4, 1259-1267 (1998).
    • (1998) RNA , vol.4 , pp. 1259-1267
    • Niederberger, N.1    Trachsel, H.2    Altmann, M.3
  • 70
    • 33747354635 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit
    • LeFebvre, A.K. et al. Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit. J. Biol. Chem. 281, 22917-22932 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 22917-22932
    • LeFebvre, A.K.1
  • 71
    • 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
    • Méthot, N., Song, M.S. & 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. 16, 5328-5334 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5328-5334
    • Méthot, N.1    Song, M.S.2    Sonenberg, N.3
  • 72
    • 0345060297 scopus 로고    scopus 로고
    • Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 5′ untranslated regions
    • Dmitriev, S.E., Terenin, I., Dunaevsky, Y., Merrick, W. & Shatsky, I. Assembly of 48S translation initiation complexes from purified components with mRNAs that have some base pairing within their 5′ untranslated regions. Mol. Cell. Biol. 23, 8925-8933 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8925-8933
    • Dmitriev, S.E.1    Terenin, I.2    Dunaevsky, Y.3    Merrick, W.4    Shatsky, I.5
  • 73
    • 33748924333 scopus 로고    scopus 로고
    • EIF3: A versatile scaffold for translation initiation complexes
    • Hinnebusch, A.G. eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem. Sci. 31, 553-562 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 553-562
    • Hinnebusch, A.G.1
  • 74
    • 33645841066 scopus 로고    scopus 로고
    • Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast
    • Nielsen, K.H., Valasek, L., Sykes, C., Jivotovskaya, A. & Hinnebusch, A.G. Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of eukaryotic initiation factor 3 in yeast. Mol. Cell. Biol. 26, 2984-2998 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2984-2998
    • Nielsen, K.H.1    Valasek, L.2    Sykes, C.3    Jivotovskaya, A.4    Hinnebusch, A.G.5
  • 75
    • 10644249220 scopus 로고    scopus 로고
    • Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP
    • Unbehaun, A., Borukhov, S.I., Hellen, C.U.T. & Pestova, T.V. Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev. 18, 3078-3093 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 3078-3093
    • Unbehaun, A.1    Borukhov, S.I.2    Hellen, C.U.T.3    Pestova, T.V.4
  • 76
    • 77956657467 scopus 로고    scopus 로고
    • The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning
    • Cuchalová, L. et al. The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning. Mol. Cell. Biol. 30, 4671-4686 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 4671-4686
    • Cuchalová, L.1
  • 77
    • 77649269977 scopus 로고    scopus 로고
    • The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection
    • Elantak, L. et al. The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection. J. Mol. Biol. 396, 1097-1116 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 1097-1116
    • Elantak, L.1
  • 78
    • 0036207282 scopus 로고    scopus 로고
    • Untranslated regions of mRNAs
    • reviews0004.1-reviews0004.10
    • Mignone, F., Gissi, C., Liuni, S. & Pesole, G. Untranslated regions of mRNAs. Genome Biol. 3, reviews0004.1-reviews0004.10 (2002).
    • (2002) Genome Biol. , vol.3
    • Mignone, F.1    Gissi, C.2    Liuni, S.3    Pesole, G.4
  • 79
    • 78149277351 scopus 로고    scopus 로고
    • Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1)
    • Ivanov, I.P., Loughran, G., Sachs, M.S. & Atkins, J.F. Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1). Proc. Natl. Acad. Sci. USA 107, 18056-18060 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18056-18060
    • Ivanov, I.P.1    Loughran, G.2    Sachs, M.S.3    Atkins, J.F.4
  • 80
    • 83255187893 scopus 로고    scopus 로고
    • Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons
    • Martin-Marcos, P., Cheung, Y.-N. & Hinnebusch, A.G. Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons. Mol. Cell. Biol. 31, 4814-4831 (2011).
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4814-4831
    • Martin-Marcos, P.1    Cheung, Y.-N.2    Hinnebusch, A.G.3
  • 82
    • 80052212313 scopus 로고    scopus 로고
    • Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation
    • Vassilenko, K.S., Alekhina, O.M., Dmitriev, S.E., Shatsky, I.N. & Spirin, A.S. Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation. Nucleic Acids Res. 39, 5555-5567 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5555-5567
    • Vassilenko, K.S.1    Alekhina, O.M.2    Dmitriev, S.E.3    Shatsky, I.N.4    Spirin, A.S.5
  • 83
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova, T.V. & Kolupaeva, V. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev. 16, 2906-2922 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.2
  • 84
    • 0345373936 scopus 로고    scopus 로고
    • Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning
    • Prévôt, D. et al. Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning. EMBO J. 22, 1909-1921 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1909-1921
    • Prévôt, D.1
  • 85
    • 77954612060 scopus 로고    scopus 로고
    • The eukaryotic initiation factor (eIF) 4G HEAT domain promotes translation re-initiation in yeast both dependent on and independent of eIF4A mRNA helicase
    • Watanabe, R. et al. The eukaryotic initiation factor (eIF) 4G HEAT domain promotes translation re-initiation in yeast both dependent on and independent of eIF4A mRNA helicase. J. Biol. Chem. 285, 21922-21933 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 21922-21933
    • Watanabe, R.1
  • 86
    • 42449155947 scopus 로고    scopus 로고
    • Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking
    • Lindqvist, L., Imataka, H. & Pelletier, J. Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking. RNA 14, 960-969 (2008).
    • (2008) RNA , vol.14 , pp. 960-969
    • Lindqvist, L.1    Imataka, H.2    Pelletier, J.3
  • 87
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function
    • von der Haar, T. & McCarthy, J.E. Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function. Mol. Microbiol. 46, 531-544 (2002).
    • (2002) Mol. Microbiol. , vol.46 , pp. 531-544
    • Von Der Haar, T.1    McCarthy, J.E.2
  • 88
    • 57649234552 scopus 로고    scopus 로고
    • Translation initiation on mammalian mRNAs with structured 5′UTRs requires DExH-box protein DHX29
    • Demonstrates that helicases besides eIF4A are required for recruitment and scanning of mRNAs containing highly stable, secondary structure elements
    • Pisareva, V.P., Pisarev, A.V., Komar, A.A., Hellen, C.U.T. & Pestova, T.V. Translation initiation on mammalian mRNAs with structured 5′UTRs requires DExH-box protein DHX29. Cell 135, 1237-1250 (2008). Demonstrates that helicases besides eIF4A are required for recruitment and scanning of mRNAs containing highly stable, secondary structure elements.
    • (2008) Cell , vol.135 , pp. 1237-1250
    • Pisareva, V.P.1    Pisarev, A.V.2    Komar, A.A.3    Hellen, C.U.T.4    Pestova, T.V.5
  • 89
    • 78650907809 scopus 로고    scopus 로고
    • Bypassing of stems versus linear base-by-base inspection of mammalian mRNAs during ribosomal scanning
    • Abaeva, I.S., Marintchev, A., Pisareva, V.P., Hellen, C.U.T. & Pestova, T.V. Bypassing of stems versus linear base-by-base inspection of mammalian mRNAs during ribosomal scanning. EMBO J. 30, 115-129 (2011).
    • (2011) EMBO J. , vol.30 , pp. 115-129
    • Abaeva, I.S.1    Marintchev, A.2    Pisareva, V.P.3    Hellen, C.U.T.4    Pestova, T.V.5
  • 90
    • 70449553011 scopus 로고    scopus 로고
    • How does a scanning ribosomal particle move along the 5′-untranslated region of eukaryotic mRNA? Brownian Ratchet model
    • Spirin, A.S. How does a scanning ribosomal particle move along the 5′-untranslated region of eukaryotic mRNA? Brownian Ratchet model. Biochemistry 48, 10688-10692 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10688-10692
    • Spirin, A.S.1
  • 91
    • 84862000545 scopus 로고    scopus 로고
    • Specific domains in yeast eIF4G strongly bias the RNA unwinding activity of the eIF4F complex towards duplexes with 5′-overhangs
    • published online, doi:10.1074/jbc.M112.347278 30 March
    • Rajagopal, V., Park, E.-H., Hinnebusch, A.G. & Lorsch, J.R. Specific domains in yeast eIF4G strongly bias the RNA unwinding activity of the eIF4F complex towards duplexes with 5′-overhangs. J. Biol. Chem. published online, doi:10.1074/jbc.M112.347278 (30 March 2012).
    • (2012) J. Biol. Chem.
    • Rajagopal, V.1    Park, E.-H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 92
    • 26944435515 scopus 로고    scopus 로고
    • Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • Algire, M.A., Maag, D. & Lorsch, J.R. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 20, 251-262 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 251-262
    • Algire, M.A.1    Maag, D.2    Lorsch, J.R.3
  • 93
    • 34249069609 scopus 로고    scopus 로고
    • Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo
    • Demonstrates the key role of eIF1 in maintaining start codon fidelity in vivo
    • Cheung, Y.-N. et al. Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo. Genes Dev. 21, 1217-1230 (2007). Demonstrates the key role of eIF1 in maintaining start codon fidelity in vivo.
    • (2007) Genes Dev. , vol.21 , pp. 1217-1230
    • Cheung, Y.-N.1
  • 94
    • 70350557033 scopus 로고    scopus 로고
    • eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation
    • Nanda, J.S. et al. eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J. Mol. Biol. 394, 268-285 (2009).
    • (2009) J. Mol. Biol. , vol.394 , pp. 268-285
    • Nanda, J.S.1
  • 95
    • 38149140938 scopus 로고    scopus 로고
    • Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection
    • Reibarkh, M. et al. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J. Biol. Chem. 283, 1094-1103 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 1094-1103
    • Reibarkh, M.1
  • 96
    • 84860181797 scopus 로고    scopus 로고
    • Stringency of start codon selection modulates autoregulation of translation initiation factor eIF5
    • Loughran, G., Sachs, M.S., Atkins, J.F. & Ivanov, I.P. Stringency of start codon selection modulates autoregulation of translation initiation factor eIF5. Nucleic Acids Res. 40, 2898-2906 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2898-2906
    • Loughran, G.1    Sachs, M.S.2    Atkins, J.F.3    Ivanov, I.P.4
  • 97
    • 31344481752 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection
    • Maag, D., Algire, M.A. & Lorsch, J.R. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. J. Mol. Biol. 356, 724-737 (2006).
    • (2006) J. Mol. Biol. , vol.356 , pp. 724-737
    • Maag, D.1    Algire, M.A.2    Lorsch, J.R.3
  • 98
    • 84863338242 scopus 로고    scopus 로고
    • Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly
    • Herrmannová, A. et al. Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly. Nucleic Acids Res. 40, 2294-2311 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 2294-2311
    • Herrmannová, A.1
  • 99
    • 0034688313 scopus 로고    scopus 로고
    • The joining of ribosomal subunits in eukaryotes requires eIF5B
    • Pestova, T.V. et al. The joining of ribosomal subunits in eukaryotes requires eIF5B. Nature 403, 332-335 (2000).
    • (2000) Nature , vol.403 , pp. 332-335
    • Pestova, T.V.1
  • 100
    • 33646852583 scopus 로고    scopus 로고
    • Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining
    • Acker, M.G., Shin, B.-S., Dever, T.E. & Lorsch, J.R. Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining. J. Biol. Chem. 281, 8469-8475 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8469-8475
    • Acker, M.G.1    Shin, B.-S.2    Dever, T.E.3    Lorsch, J.R.4
  • 101
    • 58149101175 scopus 로고    scopus 로고
    • Kinetic analysis of late steps of eukaryotic translation initiation
    • Acker, M.G. et al. Kinetic analysis of late steps of eukaryotic translation initiation. J. Mol. Biol. 385, 491-506 (2009).
    • (2009) J. Mol. Biol. , vol.385 , pp. 491-506
    • Acker, M.G.1
  • 102
    • 0037184985 scopus 로고    scopus 로고
    • Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
    • Shin, B.S. et al. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell 111, 1015-1025 (2002).
    • (2002) Cell , vol.111 , pp. 1015-1025
    • Shin, B.S.1
  • 103
    • 0037452587 scopus 로고    scopus 로고
    • Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: A new interaction between old partners
    • Marintchev, A., Kolupaeva, V., Pestova, T. & Wagner, G. Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: a new interaction between old partners. Proc. Natl. Acad. Sci. USA 100, 1535-1540 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1535-1540
    • Marintchev, A.1    Kolupaeva, V.2    Pestova, T.3    Wagner, G.4
  • 104
    • 51149091031 scopus 로고    scopus 로고
    • eIF3a cooperates with sequences 5′ of uORF1 to promote resumption of scanning by post-termination ribosomes for reinitiation on GCN4 mRNA
    • Identifies a role for eIF3 in scanning and reinitiation in vivo
    • Szamecz, B. et al. eIF3a cooperates with sequences 5′ of uORF1 to promote resumption of scanning by post-termination ribosomes for reinitiation on GCN4 mRNA. Genes Dev. 22, 2414-2425 (2008). Identifies a role for eIF3 in scanning and reinitiation in vivo.
    • (2008) Genes Dev. , vol.22 , pp. 2414-2425
    • Szamecz, B.1
  • 105
    • 36849080874 scopus 로고    scopus 로고
    • The mechanism of an exceptional case of reinitiation after translation of a long ORF reveals why such events do not generally occur in mammalian mRNA translation
    • Pöyry, T.A.A., Kaminski, A., Connell, E.J., Fraser, C.S. & Jackson, R.J. The mechanism of an exceptional case of reinitiation after translation of a long ORF reveals why such events do not generally occur in mammalian mRNA translation. Genes Dev. 21, 3149-3162 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 3149-3162
    • Pöyry, T.A.A.1    Kaminski, A.2    Connell, E.J.3    Fraser, C.S.4    Jackson, R.J.5
  • 106
    • 83855162728 scopus 로고    scopus 로고
    • The structure of the eukaryotic ribosome at 3.0 Å resolution
    • Ben-Shem, A. et al. The structure of the eukaryotic ribosome at 3.0 Å resolution. Science 334, 1524-1529 (2011).
    • (2011) Science , vol.334 , pp. 1524-1529
    • Ben-Shem, A.1
  • 107
    • 78650347088 scopus 로고    scopus 로고
    • A quantitative model for mRNA translation in Saccharomyces cerevisiae
    • You, T., Coghill, G.M. & Brown, A.J.P. A quantitative model for mRNA translation in Saccharomyces cerevisiae. Yeast 27, 785-800 (2010).
    • (2010) Yeast , vol.27 , pp. 785-800
    • You, T.1    Coghill, G.M.2    Brown, A.J.P.3
  • 108
    • 80051783478 scopus 로고    scopus 로고
    • Analysing GCN4 translational control in yeast by stochastic chemical kinetics modelling and simulation
    • You, T., Stansfield, I., Romano, M.C., Brown, A.J.P. & Coghill, G.M. Analysing GCN4 translational control in yeast by stochastic chemical kinetics modelling and simulation. BMC Syst. Biol. 5, 131 (2011).
    • (2011) BMC Syst. Biol. , vol.5 , pp. 131
    • You, T.1    Stansfield, I.2    Romano, M.C.3    Brown, A.J.P.4    Coghill, G.M.5


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