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Volumn 12, Issue 12, 2005, Pages 1145-1149

Conformational transition of initiation factor 2 from the GTP- to GDP-bound state visualized on the ribosome

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; INITIATION FACTOR 2; INITIATION FACTOR 3; MESSENGER RNA; PROTEIN SUBUNIT;

EID: 28544446738     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1012     Document Type: Article
Times cited : (121)

References (36)
  • 1
    • 0242439747 scopus 로고    scopus 로고
    • Initiation factors in the early events of mRNA translation in bacteria
    • Gualerzi, C.O. et al. Initiation factors in the early events of mRNA translation in bacteria. Cold Spring Harb. Symp. Quant. Biol. 66, 363-376 (2001).
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 363-376
    • Gualerzi, C.O.1
  • 2
    • 0035999793 scopus 로고    scopus 로고
    • Structure and function of bacterial initiation factors
    • Boelens, R. & Gualerzi, C.O. Structure and function of bacterial initiation factors. Curr. Protein Pept. Sci. 3, 107-119 (2002).
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 107-119
    • Boelens, R.1    Gualerzi, C.O.2
  • 4
    • 0034688313 scopus 로고    scopus 로고
    • The joining of ribosomal subunits in eukaryotes requires elF5B
    • Pestova, T.V. et al. The joining of ribosomal subunits in eukaryotes requires elF5B. Nature 403, 332-335 (2000).
    • (2000) Nature , vol.403 , pp. 332-335
    • Pestova, T.V.1
  • 5
    • 0035805213 scopus 로고    scopus 로고
    • Crystal structure of the ribosome at 5.5 Åresolution
    • Yusupov, M.M. et al. Crystal structure of the ribosome at 5.5 Åresolution. Science 292, 883-896 (2001).
    • (2001) Science , vol.292 , pp. 883-896
    • Yusupov, M.M.1
  • 6
    • 20144388921 scopus 로고    scopus 로고
    • Translational operator of mRNA on the ribosome: How repressor proteins exclude ribosome binding
    • Jenner, L. et al. Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding. Science 308, 120-123 (2005).
    • (2005) Science , vol.308 , pp. 120-123
    • Jenner, L.1
  • 7
    • 0034703718 scopus 로고    scopus 로고
    • X-Ray structures of the universal translation initiation factor IF2/elF5B: Conformational changes on GDP and GTP binding
    • Roll-Mecak, A., Cao, C., Dever, T.E. & Burley, S.K. X-Ray structures of the universal translation initiation factor IF2/elF5B: conformational changes on GDP and GTP binding. Cell 103, 781-792 (2000).
    • (2000) Cell , vol.103 , pp. 781-792
    • Roll-Mecak, A.1    Cao, C.2    Dever, T.E.3    Burley, S.K.4
  • 8
    • 0030770467 scopus 로고    scopus 로고
    • Visualization of elongation factor Tu on the Escherichia coli ribosome
    • Stark, H. et al. Visualization of elongation factor Tu on the Escherichia coli ribosome. Nature 389, 403-406 (1997).
    • (1997) Nature , vol.389 , pp. 403-406
    • Stark, H.1
  • 9
    • 0036646535 scopus 로고    scopus 로고
    • Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process
    • Valle, M. et al. Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. EMBO J. 21, 3557-3567 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3557-3567
    • Valle, M.1
  • 10
    • 0036829080 scopus 로고    scopus 로고
    • Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
    • Stark, H. et al. Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat. Struct. Biol. 9, 849-854 (2002).
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 849-854
    • Stark, H.1
  • 11
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation
    • Agrawal, R.K., Penczek, P., Grassucci, R.A. & Frank, J. Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation. Proc. Natl. Acad. Sci. USA 95, 6134-6138 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6134-6138
    • Agrawal, R.K.1    Penczek, P.2    Grassucci, R.A.3    Frank, J.4
  • 12
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • Stark, H., Rodnina, M.V., Wieden, H.J., van Heel, M. & Wintermeyer, W. Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell 100, 301-309 (2000).
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Van Heel, M.4    Wintermeyer, W.5
  • 13
    • 1542378898 scopus 로고    scopus 로고
    • Visualization of release factor 3 on the ribosome during termination of protein synthesis
    • Klaholz, B.P., Myasnikov, A.G. & van Heel, M. Visualization of release factor 3 on the ribosome during termination of protein synthesis. Nature 427, 862-865 (2004).
    • (2004) Nature , vol.427 , pp. 862-865
    • Klaholz, B.P.1    Myasnikov, A.G.2    Van Heel, M.3
  • 14
    • 0034903857 scopus 로고    scopus 로고
    • Initiation factor if 2 binds to the alpha-sarcin loop and helix 89 of Escherichia coli 235 ribosomal RNA
    • La Teana, A., Gualerzi, C.O. & Dahlberg, A.E. Initiation factor IF 2 binds to the alpha-sarcin loop and helix 89 of Escherichia coli 235 ribosomal RNA. RNA 7, 1173-1179 (2001).
    • (2001) RNA , vol.7 , pp. 1173-1179
    • La Teana, A.1    Gualerzi, C.O.2    Dahlberg, A.E.3
  • 15
    • 0041806480 scopus 로고    scopus 로고
    • Ribosomal localization of translation initiation factor IF2
    • Marzi, S. et al. Ribosomal localization of translation initiation factor IF2. RNA 9, 958-969 (2003).
    • (2003) RNA , vol.9 , pp. 958-969
    • Marzi, S.1
  • 16
    • 21244465843 scopus 로고    scopus 로고
    • Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation
    • Diaconu, M. et al. Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell 121, 991-1004 (2005).
    • (2005) Cell , vol.121 , pp. 991-1004
    • Diaconu, M.1
  • 17
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal, R.K., Heagle, A.B., Penczek, P., Grassucci, R.A. & Frank, J. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nat. Struct. Biol. 6, 643-647 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 18
    • 0029051704 scopus 로고
    • Specific protection of 16S rRNA by translational initiation factors
    • Moazed, D., Samaha, R.R., Gualerzi, C. & Noller, H.F. Specific protection of 16S rRNA by translational initiation factors. J. Mol. Biol. 248, 207-210 (1995).
    • (1995) J. Mol. Biol. , vol.248 , pp. 207-210
    • Moazed, D.1    Samaha, R.R.2    Gualerzi, C.3    Noller, H.F.4
  • 19
    • 0034597006 scopus 로고    scopus 로고
    • Mapping the fMet-tRNA(f)Met binding site of initiation factor IF2
    • Guenneugues, M. et al. Mapping the fMet-tRNA(f)Met) binding site of initiation factor IF2. EMBO J. 19, 5233-5240 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5233-5240
    • Guenneugues, M.1
  • 20
    • 0035910393 scopus 로고    scopus 로고
    • Crystal structure of an initiation factor bound to the 30S ribosomal subunit
    • Carter, A.P. et al. Crystal structure of an initiation factor bound to the 30S ribosomal subunit. Science 291, 498-501 (2001).
    • (2001) Science , vol.291 , pp. 498-501
    • Carter, A.P.1
  • 21
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen, G.S., Zavialov, A., Gursky, R., Ehrenberg, M. & Frank, J. The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121, 703-712 (2005).
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 22
    • 0034006565 scopus 로고    scopus 로고
    • Extremely thermostable elongation factor G from A. aeolicus: Cloning, expression, purification, and characterization in a heterologous translation system
    • Martemyanov, K.A., Liljas, A. & Gudkov, A.T. Extremely thermostable elongation factor G from A. aeolicus: cloning, expression, purification, and characterization in a heterologous translation system. Protein Expr. Purif. 18, 257-261 (2000).
    • (2000) Protein Expr. Purif. , vol.18 , pp. 257-261
    • Martemyanov, K.A.1    Liljas, A.2    Gudkov, A.T.3
  • 23
    • 0029379602 scopus 로고
    • Overexpression and purification of T. thermophilus elongation factors G, Tu, and Ts from E. coli
    • Blank, J., Grillenbeck, N.W., Kreutzer, R. & Sprinzl, M. Overexpression and purification of T. thermophilus elongation factors G, Tu, and Ts from E. coli. Protein Expr. Purif. 6, 637-645 (1995).
    • (1995) Protein Expr. Purif. , vol.6 , pp. 637-645
    • Blank, J.1    Grillenbeck, N.W.2    Kreutzer, R.3    Sprinzl, M.4
  • 24
    • 0028175534 scopus 로고
    • Purification of fMet-tRNA(fMet) by fast protein liquid chromatography
    • Rodnina, M.V., Semenkov, Y.P. & Wintermeyer, W. Purification of fMet-tRNA(fMet) by fast protein liquid chromatography. Anal. Biochem. 219, 380-381 (1994).
    • (1994) Anal. Biochem. , vol.219 , pp. 380-381
    • Rodnina, M.V.1    Semenkov, Y.P.2    Wintermeyer, W.3
  • 25
    • 0001367486 scopus 로고
    • Structure of Thermus thermophilus ribosomes. 1. Method of isolation and purification of ribosomes
    • Gogia, Z.V., Yusupov, M.M. & Spirina, T.N. Structure of Thermus thermophilus ribosomes. 1. Method of isolation and purification of ribosomes. Molekul. Biol. (USSR) 20, 519 (1986).
    • (1986) Molekul. Biol. (USSR) , vol.20 , pp. 519
    • Gogia, Z.V.1    Yusupov, M.M.2    Spirina, T.N.3
  • 26
    • 0035958587 scopus 로고    scopus 로고
    • The path of the messenger RNA through the ribosome
    • Yusupova, G.Z., Yusupov, M.M., Cate, J.H. & Noller, H.F. The path of the messenger RNA through the ribosome. Cell 106, 233 (2001).
    • (2001) Cell , vol.106 , pp. 233
    • Yusupova, G.Z.1    Yusupov, M.M.2    Cate, J.H.3    Noller, H.F.4
  • 27
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S.J., Baldwin, P.R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 28
    • 20244379996 scopus 로고    scopus 로고
    • Single-particle cryo electron microscopy: Towards atomic resolution
    • van Heel, M. et al. Single-particle cryo electron microscopy: towards atomic resolution. Q. Rev. Biophys. 33, 307-369 (2000).
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 307-369
    • Van Heel, M.1
  • 30
    • 0037413610 scopus 로고    scopus 로고
    • Structure of the Escherichia coli ribosomal termination complex with release factor 2
    • Klaholz, B.P. et al. Structure of the Escherichia coli ribosomal termination complex with release factor 2. Nature 421, 90-94 (2003).
    • (2003) Nature , vol.421 , pp. 90-94
    • Klaholz, B.P.1
  • 31
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P.B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 32
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel, M. & Schatz, M. Fourier shell correlation threshold criteria. J. Struct. Biol. 151, 250-262 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 33
    • 0043122907 scopus 로고    scopus 로고
    • PipeAlign: A new toolkit for protein family analysis
    • Plewniak, F. et al. PipeAlign: a new toolkit for protein family analysis. Nucleic Acids Res. 31, 3829-3832 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3829-3832
    • Plewniak, F.1
  • 34
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 35
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali, M. & King, R.D. Cascaded multiple classifiers for secondary structure prediction. Protein Sci. 9, 1162-1176 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 36
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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