메뉴 건너뛰기




Volumn 41, Issue 2, 2013, Pages 1047-1057

Roles of yeast eIF2α and eIF2β subunits in the binding of the initiator methionyl-tRNA

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 2ALPHA; INITIATION FACTOR 2BETA; MESSENGER RNA; METHIONINE TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84875441454     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1180     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 84861843696 scopus 로고    scopus 로고
    • A mechanistic overview of translation initiation in eukaryotes
    • Aitken, C.E. and Lorsch, J.R. (2012) A mechanistic overview of translation initiation in eukaryotes. Nat. Struct. Mol. Biol., 19, 568-576.
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 568-576
    • Aitken, C.E.1    Lorsch, J.R.2
  • 2
    • 80052742721 scopus 로고    scopus 로고
    • Molecular mechanism of scanning and start codon selection in eukaryotes
    • Hinnebusch, A.G. (2011) Molecular mechanism of scanning and start codon selection in eukaryotes. Microbiol. Mol. Biol. Rev., 75, 434-467.
    • (2011) Microbiol. Mol. Biol. Rev , vol.75 , pp. 434-467
    • Hinnebusch, A.G.1
  • 3
    • 0029858531 scopus 로고    scopus 로고
    • Ligand interactions with eukaryotic translation initiation factor 2: Role of the γ-subunit
    • Erickson, F.L. and Hannig, E.M. (1996) Ligand interactions with eukaryotic translation initiation factor 2: role of the gamma-subunit. EMBO J., 15, 6311-6320. (Pubitemid 26397904)
    • (1996) EMBO Journal , vol.15 , Issue.22 , pp. 6311-6320
    • Erickson, F.L.1    Hannig, E.M.2
  • 4
    • 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. and Lorsch, J.R. (2004) GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2. J. Mol. Biol., 335, 923-936. (Pubitemid 38091601)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 923-936
    • Kapp, L.D.1    Lorsch, J.R.2
  • 5
    • 15944425052 scopus 로고    scopus 로고
    • The archaeal eIF2 homologue: Functional properties of an ancient translation initiation factor
    • DOI 10.1093/nar/gki321
    • Pedulla, N., Palermo, R., Hasenohrl, D., Blasi, U., Cammarano, P. and Londei, P. (2005) The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor. Nucleic Acids Res., 33, 1804-1812. (Pubitemid 41748327)
    • (2005) Nucleic Acids Research , vol.33 , Issue.6 , pp. 1804-1812
    • Pedulla, N.1    Palermo, R.2    Hasenohrl, D.3    Blasi, U.4    Cammarano, P.5    Londei, P.6
  • 6
    • 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. and Schmitt, E. (2006) Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer. Structure, 14, 119-128. (Pubitemid 43350079)
    • (2006) Structure , vol.14 , Issue.1 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 7
    • 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. and Mechulam, Y. (2004) Functional molecular mapping of archaeal translation initiation factor 2. J. Biol. Chem., 279, 15984-15993. (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
  • 8
    • 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. and RajBhandary, U.L. (1996) 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. (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
  • 9
    • 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. and Mechulam, Y. (2002) The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J., 21, 1821-1832. (Pubitemid 34614638)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 10
    • 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. and Tanaka, I. (2006) Structure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 region. Proc. Natl Acad. Sci. USA, 103, 13016-13021. (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
  • 11
    • 50149109434 scopus 로고    scopus 로고
    • Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha-and beta-subunits
    • Stolboushkina, E., Nikonov, S., Nikulin, A., Blasi, U., Manstein, D.J., Fedorov, R., Garber, M. and Nikonov, O. (2008) Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha-and beta-subunits. J. Mol. Biol., 382, 680-691.
    • (2008) J. Mol. Biol , vol.382 , pp. 680-691
    • Stolboushkina, E.1    Nikonov, S.2    Nikulin, A.3    Blasi, U.4    Manstein, D.J.5    Fedorov, R.6    Garber, M.7    Nikonov, O.8
  • 14
    • 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. and Burley, S.K. (2004) X-ray structure of translation initiation factor eIF2gamma: implications for tRNA and eIF2alpha binding. J. Biol. Chem., 279, 10634-10642. (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
    • 80555131009 scopus 로고    scopus 로고
    • Initiation factor eIF2gamma promotes eIF2-GTP-Met-tRNAi(Met) ternary complex binding to the 40S ribosome
    • Shin, B.S., Kim, J.R., Walker, S.E., Dong, J., Lorsch, J.R. and Dever, T.E. (2011) Initiation factor eIF2gamma promotes eIF2-GTP-Met-tRNAi(Met) ternary complex binding to the 40S ribosome. Nat. Struct. Mol. Biol., 18, 1227-1234.
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1227-1234
    • Shin, B.S.1    Kim, J.R.2    Walker, S.E.3    Dong, J.4    Lorsch, J.R.5    Dever, T.E.6
  • 17
    • 0035846821 scopus 로고    scopus 로고
    • Biochemical analysis of the eIF2bg complex reveals a structural function for eIF2a in catalyzed nucleotide exchange
    • Nika, J., Rippel, S. and Hannig, E.M. (2001) Biochemical analysis of the eIF2bg complex reveals a structural function for eIF2a in catalyzed nucleotide exchange. J. Biol. Chem., 276, 1051-1060.
    • (2001) J. Biol. Chem , vol.276 , pp. 1051-1060
    • Nika, J.1    Rippel, S.2    Hannig, E.M.3
  • 19
    • 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. and Schmitt, E. (2010) tRNA binding properties of eukaryotic translation initiation factor 2 from Encephalitozoon cuniculi. Biochemistry, 49, 8680-8688.
    • (2010) Biochemistry , vol.49 , pp. 8680-8688
    • Naveau, M.1    Lazennec-Schurdevin, C.2    Panvert, M.3    Mechulam, Y.4    Schmitt, E.5
  • 20
    • 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. and Schmitt, E. (2007) Protection-based assays to measure aminoacyl-tRNA binding to translation initiation factors. Methods Enzymol., 430, 265-281.
    • (2007) Methods Enzymol , vol.430 , pp. 265-281
    • Mechulam, Y.1    Guillon, L.2    Yatime, L.3    Blanquet, S.4    Schmitt, E.5
  • 21
    • 0026552726 scopus 로고
    • Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAMet f formyltransferase
    • Guillon, J.M., Meinnel, T., Mechulam, Y., Lazennec, C., Blanquet, S. and Fayat, S. (1992) Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNAMet f formyltransferase. J. Mol. Biol., 224, 359-367.
    • (1992) J. Mol. Biol , vol.224 , pp. 359-367
    • Guillon, J.M.1    Meinnel, T.2    Mechulam, Y.3    Lazennec, C.4    Blanquet, S.5    Fayat, S.6
  • 22
    • 0028982837 scopus 로고
    • Maturation of pre-tRNAfMet by E. coli RNase P is specified by a guanosine of the 50 flanking sequence
    • Meinnel, T. and Blanquet, S. (1995) Maturation of pre-tRNAfMet by E. coli RNase P is specified by a guanosine of the 50 flanking sequence. J. Biol. Chem., 270, 15906-15914.
    • (1995) J. Biol. Chem , vol.270 , pp. 15906-15914
    • Meinnel, T.1    Blanquet, S.2
  • 23
    • 0024455920 scopus 로고
    • Identification of an amino acid region supporting specific methionyl-tRNA synthetase: tRNA recognition
    • Mellot, P., Mechulam, Y., LeCorre, D., Blanquet, S. and Fayat, G. (1989) Identification of an amino acid region supporting specific methionyl-tRNA synthetase:tRNA recognition. J. Mol. Biol., 208, 429-443. (Pubitemid 19220159)
    • (1989) Journal of Molecular Biology , vol.208 , Issue.3 , pp. 429-443
    • Mellot, P.1    Mechulam, Y.2    Le Corre, D.3    Blanquet, S.4    Fayat, G.5
  • 24
    • 0028242962 scopus 로고
    • MC-Fit: Using Monte-Carlo methods to get accurate confidence limits on enzyme parameters
    • Dardel, F. (1994) MC-Fit: Using Monte-Carlo methods to get accurate confidence limits on enzyme parameters. Comput. Applic. Biosci., 10, 273-275. (Pubitemid 24197992)
    • (1994) Computer Applications in the Biosciences , vol.10 , Issue.3 , pp. 273-275
    • Dardel, F.1
  • 25
    • 28244460315 scopus 로고    scopus 로고
    • Initiator tRNA binding by e/aIF5B, the eukaryotic/archaeal homologue of bacterial initiation factor IF2
    • DOI 10.1021/bi051514j
    • Guillon, L., Schmitt, E., Blanquet, S. and Mechulam, Y. (2005) Initiator tRNA binding by e/aIF5B, the eukaryotic/archaeal homologue of bacterial initiation factor IF2. Biochemistry, 44, 15594-15601. (Pubitemid 41706144)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15594-15601
    • Guillon, L.1    Schmitt, E.2    Blanquet, S.3    Mechulam, Y.4
  • 26
    • 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 Synchroron SOLEIL SWING beamline
    • David, G. and Perez, J. (2009) combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the Synchroron SOLEIL SWING beamline. J. Appl. Crystallogr., 42, 892-900.
    • (2009) J. Appl. Crystallogr , vol.42 , pp. 892-900
    • David, G.1    Perez, J.2
  • 27
  • 28
    • 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. and Koch, M.H.J. (1995) CRYSOL- A program to evaluate X-ray solution scaterring of biological macromoleucles from atomic coordinates. J. Appl. Crystallogr., 28, 768-773. (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 29
    • 0021337227 scopus 로고
    • Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis
    • Wagner, T., Gross, M. and Sigler, P.B. (1984) Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis. J. Biol. Chem., 259, 4706-4709. (Pubitemid 14144188)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.8 , pp. 4706-4709
    • Wagner, T.1    Gross, M.2    Sigler, P.B.3
  • 30
    • 33646168052 scopus 로고    scopus 로고
    • Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation
    • Kapp, L.D., Kolitz, S.E. and Lorsch, J.R. (2006) Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation. RNA, 12, 751-764.
    • (2006) RNA , vol.12 , pp. 751-764
    • Kapp, L.D.1    Kolitz, S.E.2    Lorsch, J.R.3
  • 31
    • 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. and Wagner, G. (2004) Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure Fold. Des., 12, 1693-1704. (Pubitemid 39200521)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1693-1704
    • Ito, T.1    Marintchev, A.2    Wagner, G.3
  • 32
    • 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. and Mechulam, Y. (2005) Structure-function relationships of the intact aIF2a subunit from the archaeon Pyrococcus abyssi. Biochemistry, 44, 8749-8756. (Pubitemid 40840440)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8749-8756
    • Yatime, L.1    Schmitt, E.2    Blanquet, S.3    Mechulam, Y.4
  • 33
    • 0037109034 scopus 로고    scopus 로고
    • Translation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits
    • DOI 10.1042/BJ20020556
    • Hashimoto, N.N., Carnevalli, L.S. and Castilho, B.A. (2002) Translation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits. Biochem. J., 367, 359-368. (Pubitemid 35216810)
    • (2002) Biochemical Journal , vol.367 , Issue.2 , pp. 359-368
    • Hashimoto, N.N.1    Carnevalli, L.S.2    Castilho, B.A.3
  • 34
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: New insights and challenges
    • Hinnebusch, A.G. and Lorsch, J.R. (2012) The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb. Perspect. Biol., 4, a011544.
    • (2012) Cold Spring Harb. Perspect. Biol , vol.4
    • Hinnebusch, A.G.1    Lorsch, J.R.2
  • 35
    • 15944425052 scopus 로고    scopus 로고
    • The archaeal eIF2 homologue: Functional properties of an ancient translation initiation factor
    • DOI 10.1093/nar/gki321
    • Pedulla, N., Palermo, R., Hasenohrl, D., Blasi, U., Cammarano, P. and Londei, P. (2005) The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor. Nucleic Acids Res., 33, 1804-1812. (Pubitemid 41748327)
    • (2005) Nucleic Acids Research , vol.33 , Issue.6 , pp. 1804-1812
    • Pedulla, N.1    Palermo, R.2    Hasenohrl, D.3    Blasi, U.4    Cammarano, P.5    Londei, P.6
  • 36
    • 0024297814 scopus 로고
    • Mutations at a Zn(II) finger motif in the yeast eIF-2 beta gene alter ribosomal start-site selection during the scanning process
    • Donahue, T.F., Cigan, A.M., Pabich, E.K. and Valavicius, B.C. (1988) Mutations at a Zn(II) finger motif in the yeast eIF-2 beta gene alter ribosomal start-site selection during the scanning process. Cell, 54, 621-632.
    • (1988) Cell , vol.54 , pp. 621-632
    • Donahue, T.F.1    Cigan, A.M.2    Pabich, E.K.3    Valavicius, B.C.4
  • 37
    • 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. and Donahue, T.F. (1989) Yeast translation initiation suppressor sui2 encodes the alpha subunit of eukaryotic initiation factor 2 and shares sequence identity with the human alpha subunit. Proc. Natl Acad. Sci. USA, 86, 2784-2788. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.