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Volumn 18, Issue 11, 2011, Pages 1227-1234

Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNA i Met ternary complex binding to the 40S ribosome

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATE; INITIATION FACTOR 2; METHIONINE TRANSFER RNA; RIBOSOME RNA; RNA 18S; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 80555131009     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2133     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • Schmeing, T.M. et al. The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326, 688-694 (2009).
    • (2009) Science , vol.326 , pp. 688-694
    • Schmeing, T.M.1
  • 2
    • 78149302861 scopus 로고    scopus 로고
    • The mechanism for activation of GTP hydrolysis on the ribosome
    • Voorhees, R.M., Schmeing, T.M., Kelley, A.C. & Ramakrishnan, V. The mechanism for activation of GTP hydrolysis on the ribosome. Science 330, 835-838 (2010).
    • (2010) Science , vol.330 , pp. 835-838
    • Voorhees, R.M.1    Schmeing, T.M.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 3
    • 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
  • 5
    • 0345305759 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing
    • DOI 10.1101/gad.1141803
    • Lomakin, I.B., Kolupaeva, V.G., Marintchev, A., Wagner, G. & Pestova, T.V. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev. 17, 2786-2797 (2003). (Pubitemid 37463288)
    • (2003) Genes and Development , vol.17 , Issue.22 , pp. 2786-2797
    • Lomakin, I.B.1    Kolupaeva, V.G.2    Marintchev, A.3    Wagner, G.4    Pestova, T.V.5
  • 7
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • DOI 10.1016/j.molcel.2004.11.051, PII S1097276504007737
    • Maag, D., Fekete, C.A., Gryczynski, Z. & Lorsch, J.R. 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). (Pubitemid 40138620)
    • (2005) Molecular Cell , vol.17 , Issue.2 , pp. 265-275
    • Maag, D.1    Fekete, C.A.2    Gryczynski, Z.3    Lorsch, J.R.4
  • 8
    • 69849092725 scopus 로고    scopus 로고
    • Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing
    • 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).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5167-5182
    • Yu, Y.1
  • 10
    • 73549103606 scopus 로고    scopus 로고
    • Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNAiMet binding to the ribosome
    • Saini, A.K., Nanda, J.S., Lorsch, J.R. & Hinnebusch, A.G. Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNAiMet binding to the ribosome. Genes Dev. 24, 97-110 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 97-110
    • Saini, A.K.1    Nanda, J.S.2    Lorsch, J.R.3    Hinnebusch, A.G.4
  • 11
    • 1642304746 scopus 로고    scopus 로고
    • X-ray Structure of Translation Initiation Factor eIF2: Implications for tRNA and eIF2 binding
    • DOI 10.1074/jbc.M310418200
    • Roll-Mecak, A., Alone, P., Cao, C., Dever, T.E. & Burley, S.K. X-ray structure of translation initiation factor eIF2γ: implications for tRNA and eIF2α binding. J. Biol. Chem. 279, 10634-10642 (2004). (Pubitemid 38372675)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 10634-10642
    • Roll-Mecak, A.1    Alone, P.2    Cao, C.3    Dever, T.E.4    Burley, S.K.5
  • 12
    • 0037007203 scopus 로고    scopus 로고
    • The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
    • DOI 10.1093/emboj/21.7.1821
    • Schmitt, E., Blanquet, S. & Mechulam, Y. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21, 1821-1832 (2002). (Pubitemid 34614638)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 13
    • 33748350921 scopus 로고    scopus 로고
    • Structure of archaeal translational initiation factor 2 -GDP reveals significant conformational change of the -subunit and switch 1 region
    • DOI 10.1073/pnas.0604165103
    • Sokabe, M., Yao, M., Sakai, N., Toya, S. & Tanaka, I. Structure of archaeal translational initiation factor 2βγ-GDP reveals significant conformational change of the β-subunit and switch 1 region. Proc. Natl. Acad. Sci. USA 103, 13016-13021 (2006). (Pubitemid 44338909)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.35 , pp. 13016-13021
    • Sokabe, M.1    Yao, M.2    Sakai, N.3    Toya, S.4    Tanaka, I.5
  • 14
    • 50149109434 scopus 로고    scopus 로고
    • Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the α-and β-subunits
    • Stolboushkina, E. et al. Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the α-and β-subunits. J. Mol. Biol. 382, 680-691 (2008).
    • (2008) J. Mol. Biol. , vol.382 , pp. 680-691
    • Stolboushkina, E.1
  • 15
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the subunit in an archaeal aIF2 heterodimer
    • DOI 10.1016/j.str.2005.09.020, PII S0969212605004004
    • Yatime, L., Mechulam, Y., Blanquet, S. & Schmitt, E. Structural switch of the γ subunit in an archaeal aIF2αγ heterodimer. Structure 14, 119-128 (2006). (Pubitemid 43350079)
    • (2006) Structure , vol.14 , Issue.1 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 17
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • 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).
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 18
    • 0028812785 scopus 로고
    • Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog
    • Nissen, P. et al. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 270, 1464-1472 (1995).
    • (1995) Science , vol.270 , pp. 1464-1472
    • Nissen, P.1
  • 19
    • 0025815046 scopus 로고
    • The 3 A crystal structure of yeast initiator tRNA: Functional implications in initiator/elongator discrimination
    • Basavappa, R. & Sigler, P.B. The 3 Å crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination. EMBO J. 10, 3105-3111 (1991). (Pubitemid 21905332)
    • (1991) EMBO Journal , vol.10 , Issue.10 , pp. 3105-3111
    • Basavappa, R.1    Sigler, P.B.2
  • 20
    • 78649426085 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic ribosome
    • Ben-Shem, A., Jenner, L., Yusupova, G. & Yusupov, M. Crystal structure of the eukaryotic ribosome. Science 330, 1203-1209 (2010).
    • (2010) Science , vol.330 , pp. 1203-1209
    • Ben-Shem, A.1    Jenner, L.2    Yusupova, G.3    Yusupov, M.4
  • 22
    • 0029022224 scopus 로고
    • Mutations in GCD11, the structural gene for eIF-2γ in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis
    • Dorris, D.R., Erickson, F.L. & Hannig, E.M. Mutations in GCD11, the structural gene for eIF-2γ in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis. EMBO J. 14, 2239-2249 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2239-2249
    • Dorris, D.R.1    Erickson, F.L.2    Hannig, E.M.3
  • 23
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • DOI 10.1146/annurev.micro.59.031805.133833
    • Hinnebusch, A.G. Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59, 407-450 (2005). (Pubitemid 41507438)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 24
    • 0022817680 scopus 로고
    • Multiple GCD genes required for repression of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae
    • Harashima, S. & Hinnebusch, A.G. Multiple GCD genes required for repression of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 6, 3990-3998 (1986).
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3990-3998
    • Harashima, S.1    Hinnebusch, A.G.2
  • 25
    • 0029858531 scopus 로고    scopus 로고
    • Ligand interactions with eukaryotic translation initiation factor 2: Role of the -subunit
    • Erickson, F.L. & Hannig, E.M. Ligand interactions with eukaryotic translation initiation factor 2: role of the γ-subunit. EMBO J. 15, 6311-6320 (1996). (Pubitemid 26397904)
    • (1996) EMBO Journal , vol.15 , Issue.22 , pp. 6311-6320
    • Erickson, F.L.1    Hannig, E.M.2
  • 26
    • 33947324018 scopus 로고    scopus 로고
    • Phe
    • DOI 10.1016/j.jmb.2007.01.075, PII S0022283607001404
    • Sanderson, L.E. & Uhlenbeck, O.C. Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe. J. Mol. Biol. 368, 119-130 (2007). (Pubitemid 46441218)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.1 , pp. 119-130
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 27
    • 34248993209 scopus 로고    scopus 로고
    • The 51-63 base pair of tRNA confers specificity for binding by EF-Tu
    • DOI 10.1261/rna.485307
    • Sanderson, L.E. & Uhlenbeck, O.C. The 51-63 base pair of tRNA confers specificity for binding by EF-Tu. RNA 13, 835-840 (2007). (Pubitemid 46799817)
    • (2007) RNA , vol.13 , Issue.6 , pp. 835-840
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 28
    • 50049130690 scopus 로고    scopus 로고
    • Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNAMet and AUG selection
    • Dong, J. et al. Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNAMet and AUG selection. Genes Dev. 22, 2242-2255 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 2242-2255
    • Dong, J.1
  • 29
    • 33644779804 scopus 로고    scopus 로고
    • +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
    • DOI 10.1101/gad.1397906
    • Pisarev, A.V. et al. Specific functional interactions of nucleotides at key 3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev. 20, 624-636 (2006). (Pubitemid 43345327)
    • (2006) Genes and Development , vol.20 , Issue.5 , pp. 624-636
    • Pisarev, A.V.1    Kolupaeva, V.G.2    Pisareva, V.P.3    Merrick, W.C.4    Hellen, C.U.T.5    Pestova, T.V.6
  • 30
    • 0033963789 scopus 로고    scopus 로고
    • The eIF1A solution structure reveals a large RNA-binding surface important for scanning function
    • Battiste, J.L., Pestova, T.V., Hellen, C.U.T. & Wagner, G. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol. Cell 5, 109-119 (2000). (Pubitemid 30105440)
    • (2000) Molecular Cell , vol.5 , Issue.1 , pp. 109-119
    • Battiste, J.L.1    Pestova, T.V.2    Hellen, C.U.T.3    Wagner, G.4
  • 33
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the post-translocational state
    • Gao, Y.G. et al. The structure of the ribosome with elongation factor G trapped in the post-translocational state. Science 326, 694-699 (2009).
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1
  • 34
    • 59249086519 scopus 로고    scopus 로고
    • RRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit
    • Shin, B.S. et al. rRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit. Mol. Cell. Biol. 29, 808-821 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 808-821
    • Shin, B.S.1
  • 35
    • 52149112910 scopus 로고    scopus 로고
    • Structure of the 30S translation initiation complex
    • Simonetti, A. et al. Structure of the 30S translation initiation complex. Nature 455, 416-420 (2008).
    • (2008) Nature , vol.455 , pp. 416-420
    • Simonetti, A.1
  • 36
    • 34447302886 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing
    • DOI 10.1038/sj.emboj.7601751, PII 7601751
    • Unbehaun, A. et al. Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing. EMBO J. 26, 3109-3123 (2007). (Pubitemid 47057491)
    • (2007) EMBO Journal , vol.26 , Issue.13 , pp. 3109-3123
    • Unbehaun, A.1    Marintchev, A.2    Lomakin, I.B.3    Didenko, T.4    Wagner, G.5    Hellen, C.U.T.6    Pestova, T.V.7
  • 37
    • 1942437572 scopus 로고    scopus 로고
    • Functional Molecular Mapping of Archaeal Translation Initiation Factor 2
    • DOI 10.1074/jbc.M311561200
    • Yatime, L., Schmitt, E., Blanquet, S. & Mechulam, Y. Functional molecular mapping of archaeal translation initiation factor 2. J. Biol. Chem. 279, 15984-15993 (2004). (Pubitemid 38509287)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 15984-15993
    • Yatime, L.1    Schmitt, E.2    Blanquet, S.3    Mechulam, Y.4
  • 40
    • 0028034499 scopus 로고
    • Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination
    • DOI 10.1016/0092-8674(94)90262-3
    • Aström, S.U. & Byström, A.S. Rit, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination. Cell 79, 535-546 (1994). (Pubitemid 24346068)
    • (1994) Cell , vol.79 , Issue.3 , pp. 535-546
    • Astrom, S.U.1    Bystrom, A.S.2
  • 41
    • 0027340369 scopus 로고
    • The yeast initiator tRNA(Met) can act as an elongator tRNA(Met) in vivo
    • DOI 10.1006/jmbi.1993.1483
    • Aström, S.U., von Pawel-Rammingen, U. & Bystrom, A.S. The yeast initiator tRNAMet can act as an elongator tRNAMet in vivo. J. Mol. Biol. 233, 43-58 (1993). (Pubitemid 23288910)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.1 , pp. 43-58
    • Astrom, S.U.1    Von Pawel-Rammingen, U.2    Bystrom, A.S.3
  • 42
    • 2442697841 scopus 로고    scopus 로고
    • The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid
    • DOI 10.1021/bi036290o
    • Dale, T., Sanderson, L.E. & Uhlenbeck, O.C. The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid. Biochemistry 43, 6159-6166 (2004). (Pubitemid 38669484)
    • (2004) Biochemistry , vol.43 , Issue.20 , pp. 6159-6166
    • Dale, T.1    Sanderson, L.E.2    Uhlenbeck, O.C.3
  • 43
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • DOI 10.1126/science.1064242
    • LaRiviere, F.J., Wolfson, A.D. & Uhlenbeck, O.C. Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science 294, 165-168 (2001). (Pubitemid 32952970)
    • (2001) Science , vol.294 , Issue.5540 , pp. 165-168
    • LaRiviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 44
    • 0347123543 scopus 로고    scopus 로고
    • GTP-dependent Recognition of the Methionine Moiety on Initiator tRNA by Translation Factor eIF2
    • DOI 10.1016/j.jmb.2003.11.025
    • Kapp, L.D. & Lorsch, J.R. GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2. J. Mol. Biol. 335, 923-936 (2004). (Pubitemid 38091601)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 923-936
    • Kapp, L.D.1    Lorsch, J.R.2
  • 45
    • 0021846299 scopus 로고
    • A hierarchy of trans-acting factors modulates translation of an activator of amino acid biosynthetic genes in Saccharomyces cerevisiae
    • Hinnebusch, A.G. A hierarchy of trans-acting factors modulate translation of an activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 5, 2349-2360 (1985). (Pubitemid 15014520)
    • (1985) Molecular and Cellular Biology , vol.5 , Issue.9 , pp. 2349-2360
    • Hinnebusch, A.G.1
  • 46
    • 0033655152 scopus 로고    scopus 로고
    • Directed hydroxyl radical probing of RNA from iron(II) tethered to proteins in ribonucleoprotein complexes
    • Culver, G.M. & Noller, H.F. Directed hydroxyl radical probing of RNA from iron(II) tethered to proteins in ribonucleoprotein complexes. Methods Enzymol. 318, 461-475 (2000). (Pubitemid 30421666)
    • (2000) Methods in Enzymology , vol.318 , pp. 461-475
    • Culver, G.M.1    Noller, H.F.2
  • 47
    • 0033582628 scopus 로고    scopus 로고
    • A computational screen for methylation guide snoRNAs in yeast
    • Lowe, T.M. & Eddy, S.R. A computational screen for methylation guide snoRNAs in yeast. Science 283, 1168-1171 (1999).
    • (1999) Science , vol.283 , pp. 1168-1171
    • Lowe, T.M.1    Eddy, S.R.2
  • 48


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