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Volumn 110, Issue 39, 2013, Pages 15662-15667

Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 5B; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84884645185     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1309360110     Document Type: Article
Times cited : (24)

References (43)
  • 1
    • 33846887420 scopus 로고    scopus 로고
    • Phylogenetic distribution of translational GTPases in bacteria
    • Margus T, Remm M, Tenson T (2007) Phylogenetic distribution of translational GTPases in bacteria. BMC Genomics 8:15.
    • (2007) BMC Genomics , vol.8 , pp. 15
    • Margus, T.1    Remm, M.2    Tenson, T.3
  • 3
    • 0018577166 scopus 로고
    • Specific interaction of initiation factor IF2 of E. Coli with formylmethionyl-tRNA f Met
    • Petersen HU, Røll T, Grunberg-Manago M, Clark BF (1979) Specific interaction of initiation factor IF2 of E. Coli with formylmethionyl-tRNA f Met. Biochem Biophys Res Commun 91(3):1068-1074.
    • (1979) Biochem Biophys Res Commun , vol.91 , Issue.3 , pp. 1068-1074
    • Petersen, H.U.1    Røll, T.2    Grunberg-Manago, M.3    Clark, B.F.4
  • 4
    • 0034723404 scopus 로고    scopus 로고
    • The C-terminal subdomain (IF2 C-2) contains the entire fMettRNA binding site of initiation factor IF2
    • Spurio R, et al. (2000) The C-terminal subdomain (IF2 C-2) contains the entire fMettRNA binding site of initiation factor IF2. J Biol Chem 275(4):2447-2454.
    • (2000) J Biol Chem , vol.275 , Issue.4 , pp. 2447-2454
    • Spurio, R.1
  • 5
    • 0029913289 scopus 로고    scopus 로고
    • Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P-site
    • La Teana A, Pon CL, Gualerzi CO (1996) Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P-site. J Mol Biol 256(4):667-675.
    • (1996) J Mol Biol , vol.256 , Issue.4 , pp. 667-675
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 6
    • 52149112910 scopus 로고    scopus 로고
    • Structure of the 30S translation initiation complex
    • Simonetti A, et al. (2008) Structure of the 30S translation initiation complex. Nature 455(7211):416-420.
    • (2008) Nature , vol.455 , Issue.7211 , pp. 416-420
    • Simonetti, A.1
  • 7
    • 79960917084 scopus 로고    scopus 로고
    • The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli
    • Julián P, et al. (2011) The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli. PLoS Biol 9(7):e1001095.
    • (2011) PLoS Biol , vol.9 , Issue.7
    • Julián, P.1
  • 8
    • 0015927308 scopus 로고
    • Effect of ribosomal protein L12 upon initiation factor IF-2 activities
    • Kay A, Sander G, Grunberg-Manago M (1973) Effect of ribosomal protein L12 upon initiation factor IF-2 activities. Biochem Biophys Res Commun 51(4):979-986.
    • (1973) Biochem Biophys Res Commun , vol.51 , Issue.4 , pp. 979-986
    • Kay, A.1    Sander, G.2    Grunberg-Manago, M.3
  • 9
    • 28544446738 scopus 로고    scopus 로고
    • Conformational transition of initiation factor 2 from the GTP-to GDP-bound state visualized on the ribosome
    • Myasnikov AG, et al. (2005) Conformational transition of initiation factor 2 from the GTP-to GDP-bound state visualized on the ribosome. Nat Struct Mol Biol 12(12): 1145-1149.
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.12 , pp. 1145-1149
    • Myasnikov, A.G.1
  • 10
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J (2005) The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121(5):703-712.
    • (2005) Cell , vol.121 , Issue.5 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 11
    • 55749099506 scopus 로고    scopus 로고
    • Irreversible chemical steps control intersubunit dynamics during translation
    • Marshall RA, Dorywalska M, Puglisi JD (2008) Irreversible chemical steps control intersubunit dynamics during translation. Proc Natl Acad Sci USA 105(40):15364-15369.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.40 , pp. 15364-15369
    • Marshall, R.A.1    Dorywalska, M.2    Puglisi, J.D.3
  • 12
    • 0038182530 scopus 로고    scopus 로고
    • A conserved structural motif at the N terminus of bacterial translation initiation factor IF2
    • Laursen BS, Mortensen KK, Sperling-Petersen HU, Hoffman DW (2003) A conserved structural motif at the N terminus of bacterial translation initiation factor IF2. J Biol Chem 278(18):16320-16328.
    • (2003) J Biol Chem , vol.278 , Issue.18 , pp. 16320-16328
    • Laursen, B.S.1    Mortensen, K.K.2    Sperling-Petersen, H.U.3    Hoffman, D.W.4
  • 13
    • 84859508471 scopus 로고    scopus 로고
    • Structural dynamics of bacterial translation initiation factor IF2
    • Wienk H, et al. (2012) Structural dynamics of bacterial translation initiation factor IF2. J Biol Chem 287(14):10922-10932.
    • (2012) J Biol Chem , vol.287 , Issue.14 , pp. 10922-10932
    • Wienk, H.1
  • 14
    • 24344440731 scopus 로고    scopus 로고
    • Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2
    • Wienk H, et al. (2005) Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2. Protein Sci 14(9):2461-2468.
    • (2005) Protein Sci , vol.14 , Issue.9 , pp. 2461-2468
    • Wienk, H.1
  • 15
    • 0034678924 scopus 로고    scopus 로고
    • Structure of the fMet-tRNA(fMet)-binding domain of B. Stearothermophilus initiation factor IF2
    • Meunier S, et al. (2000) Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2. EMBO J 19(8):1918-1926.
    • (2000) EMBO J , vol.19 , Issue.8 , pp. 1918-1926
    • Meunier, S.1
  • 16
    • 43949083746 scopus 로고    scopus 로고
    • Solution structure of C-terminal Escherichia coli translation initiation factor IF2 by small-angle X-ray scattering
    • Rasmussen LC, et al. (2008) Solution structure of C-terminal Escherichia coli translation initiation factor IF2 by small-angle X-ray scattering. Biochemistry 47(20):5590-5598.
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5590-5598
    • Rasmussen, L.C.1
  • 17
    • 84884635539 scopus 로고    scopus 로고
    • Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor
    • Simonetti A, et al. (2013) Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor. Proc Natl Acad Sci USA 110:15656-15661.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 15656-15661
    • Simonetti, A.1
  • 18
    • 84878313058 scopus 로고    scopus 로고
    • Structure of the protein core of translation initiation factor IF2 in apo, GTP and GDP forms
    • Simonetti AMS, et al. (2013) Structure of the protein core of translation initiation factor IF2 in apo, GTP and GDP forms. Acta Crystallogr D Biol Crystallogr 69(6):925-33.
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , Issue.6 , pp. 925-933
    • Simonetti, A.M.S.1
  • 19
    • 0033039626 scopus 로고    scopus 로고
    • Characterization of the domains of E. Coli initiation factor IF2 responsible for recognition of the ribosome
    • Moreno JM, Drskjøtersen L, Kristensen JE, Mortensen KK, Sperling-Petersen HU (1999) Characterization of the domains of E. Coli initiation factor IF2 responsible for recognition of the ribosome. FEBS Lett 455(1-2):130-134.
    • (1999) FEBS Lett , vol.455 , Issue.1-2 , pp. 130-134
    • Moreno, J.M.1    Drskjøtersen, L.2    Kristensen, J.E.3    Mortensen, K.K.4    Sperling-Petersen, H.U.5
  • 20
    • 74649084177 scopus 로고    scopus 로고
    • Ribosomal interaction of Bacillus stearothermophilus translation initiation factor IF2: Characterization of the active sites
    • Caserta E, et al. (2010) Ribosomal interaction of Bacillus stearothermophilus translation initiation factor IF2: Characterization of the active sites. J Mol Biol 396(1):118-129.
    • (2010) J Mol Biol , vol.396 , Issue.1 , pp. 118-129
    • Caserta, E.1
  • 21
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • Schmeing TM, et al. (2009) The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326(5953):688-694.
    • (2009) Science , vol.326 , Issue.5953 , pp. 688-694
    • Schmeing, T.M.1
  • 22
    • 56749096848 scopus 로고    scopus 로고
    • Translation initiation factor IF1 of Bacillus stearothermophilus and Thermus thermophilus substitute for Escherichia coli IF1 in vivo and in vitro without a direct IF1-IF2 interaction
    • Kapralou S, et al. (2008) Translation initiation factor IF1 of Bacillus stearothermophilus and Thermus thermophilus substitute for Escherichia coli IF1 in vivo and in vitro without a direct IF1-IF2 interaction. Mol Microbiol 70(6):1368-1377.
    • (2008) Mol Microbiol , vol.70 , Issue.6 , pp. 1368-1377
    • Kapralou, S.1
  • 23
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang SR (1997) G protein mechanisms: Insights from structural analysis. Annu Rev Biochem 66:639-678.
    • (1997) Annu Rev Biochem , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 26
    • 0034703718 scopus 로고    scopus 로고
    • X-Ray structures of the universal translation initiation factor IF2/eIF5B: Conformational changes on GDP and GTP binding
    • Roll-Mecak A, Cao C, Dever TE, Burley SK (2000) X-Ray structures of the universal translation initiation factor IF2/eIF5B: Conformational changes on GDP and GTP binding. Cell 103(5):781-792.
    • (2000) Cell , vol.103 , Issue.5 , pp. 781-792
    • Roll-Mecak, A.1    Cao, C.2    Dever, T.E.3    Burley, S.K.4
  • 27
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F (1991) The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349(6305):117-127.
    • (1991) Nature , vol.349 , Issue.6305 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 28
    • 0342264747 scopus 로고    scopus 로고
    • Late events of translation initiation in bacteria: A kinetic analysis
    • Tomsic J, et al. (2000) Late events of translation initiation in bacteria: A kinetic analysis. EMBO J 19(9):2127-2136.
    • (2000) EMBO J , vol.19 , Issue.9 , pp. 2127-2136
    • Tomsic, J.1
  • 29
    • 50349097986 scopus 로고    scopus 로고
    • Cofactor dependent conformational switching of GTPases
    • Hauryliuk V, Hansson S, Ehrenberg M (2008) Cofactor dependent conformational switching of GTPases. Biophys J 95(4):1704-1715.
    • (2008) Biophys J , vol.95 , Issue.4 , pp. 1704-1715
    • Hauryliuk, V.1    Hansson, S.2    Ehrenberg, M.3
  • 30
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov AV, Buckingham RH, Ehrenberg M (2001) A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell 107(1):115-124.
    • (2001) Cell , vol.107 , Issue.1 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 31
    • 20444393817 scopus 로고    scopus 로고
    • Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs
    • Zavialov AV, Hauryliuk VV, Ehrenberg M (2005) Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs. J Biol 4(2):9.
    • (2005) J Biol , vol.4 , Issue.2 , pp. 9
    • Zavialov, A.V.1    Hauryliuk, V.V.2    Ehrenberg, M.3
  • 32
    • 0033525871 scopus 로고    scopus 로고
    • In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2
    • Luchin S, et al. (1999) In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2. Direct evidence that GTP hydrolysis is necessary for factor recycling. J Biol Chem 274(10):6074-6079.
    • (1999) Direct Evidence That GTP Hydrolysis Is Necessary for Factor Recycling. J Biol Chem , vol.274 , Issue.10 , pp. 6074-6079
    • Luchin, S.1
  • 33
    • 0142041880 scopus 로고    scopus 로고
    • The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis
    • Antoun A, Pavlov MY, Andersson K, Tenson T, Ehrenberg M (2003) The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis. EMBO J 22(20):5593-5601.
    • (2003) EMBO J , vol.22 , Issue.20 , pp. 5593-5601
    • Antoun, A.1    Pavlov, M.Y.2    Andersson, K.3    Tenson, T.4    Ehrenberg, M.5
  • 34
    • 33749021074 scopus 로고    scopus 로고
    • The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor
    • Milon P, et al. (2006) The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor. Proc Natl Acad Sci USA 103(38):13962-13967.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.38 , pp. 13962-13967
    • Milon, P.1
  • 35
    • 2342547059 scopus 로고    scopus 로고
    • Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering
    • Antoun A, Pavlov MY, Tenson T, Ehrenberg M (2004) Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering. Biol Proced Online 6: 35-54.
    • (2004) Biol Proced Online , vol.6 , pp. 35-54
    • Antoun, A.1    Pavlov, M.Y.2    Tenson, T.3    Ehrenberg, M.4
  • 36
    • 77950371305 scopus 로고    scopus 로고
    • The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex
    • Milon P, et al. (2010) The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complex. EMBO Rep 11(4):312-316.
    • (2010) EMBO Rep , vol.11 , Issue.4 , pp. 312-316
    • Milon, P.1
  • 37
    • 84863986007 scopus 로고    scopus 로고
    • Heterogeneous pathways and timing of factor departure during translation initiation
    • Tsai A, et al. (2012) Heterogeneous pathways and timing of factor departure during translation initiation. Nature 487(7407):390-393.
    • (2012) Nature , vol.487 , Issue.7407 , pp. 390-393
    • Tsai, A.1
  • 38
    • 0015167209 scopus 로고
    • A complex between initiation factor IF2, guanosine triphosphate, and fMet-tRNA: An intermediate in initiation complex formation
    • Lockwood AH, Chakraborty PR, Maitra U (1971) A complex between initiation factor IF2, guanosine triphosphate, and fMet-tRNA: An intermediate in initiation complex formation. Proc Natl Acad Sci USA 68(12):3122-3126.
    • (1971) Proc Natl Acad Sci USA , vol.68 , Issue.12 , pp. 3122-3126
    • Lockwood, A.H.1    Chakraborty, P.R.2    Maitra, U.3
  • 39
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182(2):319-326.
    • (1989) Anal Biochem , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol: Macromolec Crystallogr A 276:307-326.
    • (1997) Methods Enzymol: Macromolec Crystallogr A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(Pt 4):235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , Issue.PART 4 , pp. 235-242
    • Winn, M.D.1
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1


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