메뉴 건너뛰기




Volumn 19, Issue 4, 2012, Pages 450-454

Structure of the ternary initiation complex aIF2-GDPNP-methionylated initiator tRNA

Author keywords

[No Author keywords available]

Indexed keywords

AIF2 PROTEIN; AIF2 PROTEIN GAMMA; BACTERIAL PROTEIN; ELONGATION FACTOR 1ALPHA; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; TRANSFER RNA; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; ARCHAEAL RNA; DRUG DERIVATIVE; GDPNP COMPOUND; INITIATION FACTOR; INITIATION FACTOR 2, ARCHAEAL; METHIONINE TRANSFER RNA;

EID: 84861321529     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2259     Document Type: Article
Times cited : (55)

References (46)
  • 1
    • 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
  • 2
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson, R.J., Hellen, C.U. & 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.2    Pestova, T.V.3
  • 3
    • 26944435515 scopus 로고    scopus 로고
    • i release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • DOI 10.1016/j.molcel.2005.09.008, PII S1097276505016084
    • 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). (Pubitemid 41484170)
    • (2005) Molecular Cell , vol.20 , Issue.2 , pp. 251-262
    • Algire, M.A.1    Maag, D.2    Lorsch, J.R.3
  • 4
    • 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
    • DOI 10.1101/gad.1255704
    • Unbehaun, A., Borukhov, S.I., Hellen, C.U. & 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). (Pubitemid 39658176)
    • (2004) Genes and Development , vol.18 , Issue.24 , pp. 3078-3093
    • Unbehaun, A.1    Borukhov, S.I.2    Hellen, C.U.T.3    Pestova, T.V.4
  • 5
    • 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
  • 6
    • 0029858531 scopus 로고    scopus 로고
    • Ligand interactions with eukaryotic translation initiation factor 2: Role of the γ-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
  • 7
    • 0030886675 scopus 로고    scopus 로고
    • GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae
    • Huang, H.K., Yoon, H., Hannig, E.M. & Donahue, T.F. GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae. Genes Dev. 11, 2396-2413 (1997). (Pubitemid 27408536)
    • (1997) Genes and Development , vol.11 , Issue.18 , pp. 2396-2413
    • Huang, H.-K.1    Yoon, H.2    Hannig, E.M.3    Donahue, T.F.4
  • 8
    • 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
  • 9
  • 10
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the γ subunit in an archaeal aIF2αγ 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
  • 11
    • 0035846821 scopus 로고    scopus 로고
    • Biochemical analysis of the eIF2βγ complex reveals a structural function for eIF2α in catalyzed nucleotide exchange
    • DOI 10.1074/jbc.M007398200
    • Nika, J., Rippel, S. & Hannig, E.M. Biochemical analysis of the eIF2βγ complex reveals a structural function for eIF2α in catalyzed nucleotide exchange. J. Biol. Chem. 276, 1051-1056 (2001). (Pubitemid 32096527)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 1051-1056
    • Nika, J.1    Rippel, S.2    Hannig, E.M.3
  • 12
    • 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
  • 13
    • 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
  • 15
    • 1642304746 scopus 로고    scopus 로고
    • X-ray Structure of Translation Initiation Factor eIF2γ: Implications for tRNA and eIF2α 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
  • 16
    • 33748350921 scopus 로고    scopus 로고
    • Structure of archaeal translational initiation factor 2 βγ-GDP reveals significant conformational change of the β-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 2 βγ-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
  • 17
    • 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
  • 18
    • 71849102917 scopus 로고    scopus 로고
    • Eukaryotic and archaeal translation initiation factor 2: A heterotrimeric tRNA carrier
    • Schmitt, E., Naveau, M. & Mechulam, Y. Eukaryotic and archaeal translation initiation factor 2: a heterotrimeric tRNA carrier. FEBS Lett. 584, 405-412 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 405-412
    • Schmitt, E.1    Naveau, M.2    Mechulam, Y.3
  • 19
    • 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
  • 21
    • 80555131009 scopus 로고    scopus 로고
    • Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAiMet ternary complex binding to the 40S ribosome
    • Shin, B.S. et al. Initiation factor eIF2γ promotes eIF2-GTP-Met-tRNAiMet ternary complex binding to the 40S ribosome. Nat. Struct. Mol. Biol. 18, 1227-1234 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1227-1234
    • Shin, B.S.1
  • 22
    • 0032404016 scopus 로고    scopus 로고
    • Crystal structure of methionyl-tRNA(f)(Met) transformylase complexed with the initiator formyl-methionyl-tRNA(f)(Met)
    • Schmitt, E., Panvert, M., Blanquet, S. & Mechulam, Y. Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet. EMBO J. 17, 6819-6826 (1998). (Pubitemid 28550275)
    • (1998) EMBO Journal , vol.17 , Issue.23 , pp. 6819-6826
    • Schmitt, E.1    Panvert, M.2    Blanquet, S.3    Mechulam, Y.4
  • 23
    • 4444333127 scopus 로고    scopus 로고
    • Solution structure of human initiation factor eIF2α reveals homology to the elongation factor eEF1B
    • DOI 10.1016/j.str.2004.07.010, PII S0969212604002795
    • Ito, T., Marintchev, A. & Wagner, G. Solution structure of human initiation factor eIF2α reveals homology to the elongation factor eEF1B. Structure 12, 1693-1704 (2004). (Pubitemid 39200521)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1693-1704
    • Ito, T.1    Marintchev, A.2    Wagner, G.3
  • 24
    • 20544464681 scopus 로고    scopus 로고
    • Structure - Function relationships of the intact aIF2α subunit from the archaeon Pyrococcus abyssi
    • DOI 10.1021/bi050373i
    • Yatime, L., Schmitt, E., Blanquet, S. & Mechulam, Y. Structure-function relationships of the intact aIF2α subunit from the archaeon Pyrococcus abyssi. Biochemistry 44, 8749-8756 (2005). (Pubitemid 40840440)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8749-8756
    • Yatime, L.1    Schmitt, E.2    Blanquet, S.3    Mechulam, Y.4
  • 25
    • 0029666095 scopus 로고    scopus 로고
    • The A1 · U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2
    • Farruggio, D., Chaudhuri, J., Maitra, U. & RajBhandary, U.L. The A1 x U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2. Mol. Cell. Biol. 16, 4248-4256 (1996). (Pubitemid 26251226)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.8 , pp. 4248-4256
    • Farruggio, D.1    Chaudhuri, J.2    Maitra, U.3    Rajbhandary, U.L.4
  • 26
    • 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
  • 27
    • 0024297814 scopus 로고
    • Mutations at a Zn(II) finger motif in the yeast eIF-2β gene alter ribosomal start-site selection during the scanning process
    • Donahue, T.F., Cigan, A.M., Pabich, E.K. & Valavicius, B.C. Mutations at a Zn(II) finger motif in the yeast eIF-2β gene alter ribosomal start-site selection during the scanning process. Cell 54, 621-632 (1988).
    • (1988) Cell , vol.54 , pp. 621-632
    • Donahue, T.F.1    Cigan, A.M.2    Pabich, E.K.3    Valavicius, B.C.4
  • 28
    • 0013112952 scopus 로고
    • Yeast translation initiation suppressor sui2 encodes the α subunit of eukaryotic initiation factor 2 and shares sequence identity with the human α subunit
    • DOI 10.1073/pnas.86.8.2784
    • Cigan, A.M., Pabich, E.K., Feng, L. & Donahue, T.F. Yeast translation initiation suppressor sui2 encodes the α subunit of eukaryotic initiation factor 2 and shares sequence identity with the human α subunit. Proc. Natl. Acad. Sci. USA 86, 2784-2788 (1989). (Pubitemid 19112625)
    • (1989) Proceedings of the National Academy of Sciences of the United States of America , vol.86 , Issue.8 , pp. 2784-2788
    • Cigan, A.M.1    Pabich, E.K.2    Feng, L.3    Donahue, T.F.4
  • 29
    • 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
  • 31
    • 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
  • 32
    • 79960917084 scopus 로고    scopus 로고
    • The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli
    • Julián, P. et al. The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. PLoS Biol. 9, e1001095 (2011).
    • (2011) PLoS Biol. , vol.9
    • Julián, P.1
  • 33
    • 0032510912 scopus 로고    scopus 로고
    • Promotion of Met-tRNA(i)/(Met) binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast
    • DOI 10.1126/science.280.5370.1757
    • Choi, S.K., Lee, J.H., Zoll, W.L., Merrick, W.C. & Dever, T.E. Promotion of met-tRNAiMet binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast. Science 280, 1757-1760 (1998). (Pubitemid 28283500)
    • (1998) Science , vol.280 , Issue.5370 , pp. 1757-1760
    • Choi, S.K.1    Lee, J.H.2    Zoll, W.L.3    Merrick, W.C.4    Dever, T.E.5
  • 36
    • 38449087034 scopus 로고    scopus 로고
    • Protection-based assays to measure aminoacyl-tRNA binding to translation initiation factors
    • Mechulam, Y., Guillon, L., Yatime, L., Blanquet, S. & Schmitt, E. Protection-based assays to measure aminoacyl-tRNA binding to translation initiation factors. Methods Enzymol. 430, 265-281 (2007).
    • (2007) Methods Enzymol. , vol.430 , pp. 265-281
    • Mechulam, Y.1    Guillon, L.2    Yatime, L.3    Blanquet, S.4    Schmitt, E.5
  • 37
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W.J. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21, 916-924 (1988).
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.J.1
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 40
    • 50849106034 scopus 로고    scopus 로고
    • A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis
    • Barraud, P., Schmitt, E., Mechulam, Y., Dardel, F. & Tisne, C. A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis. Nucleic Acids Res. 36, 4894-4901 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4894-4901
    • Barraud, P.1    Schmitt, E.2    Mechulam, Y.3    Dardel, F.4    Tisne, C.5
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 43
  • 44
    • 70349316826 scopus 로고    scopus 로고
    • Combined sampler robot and high-performance liquid chromatography: A fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline
    • David, G. & Perez, J. Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline. J. Appl. Crystallogr. 42, 892-900 (2009).
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 892-900
    • David, G.1    Perez, J.2
  • 46
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D.I., Barberato, C. & Koch, M.H.J. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995). (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.