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Volumn 95, Issue 4, 2008, Pages 1704-1715

Cofactor dependent conformational switching of GTPases

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE;

EID: 50349097986     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.127290     Document Type: Article
Times cited : (32)

References (84)
  • 1
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang, S. R. 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
  • 2
    • 0029654105 scopus 로고
    • GTPases: A family of molecular switches and clocks
    • Bourne, H. R. 1995. GTPases: a family of molecular switches and clocks. Philos. Trans. R. Soc. Lond. B Biol. Sci. 349:283-289.
    • (1995) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.349 , pp. 283-289
    • Bourne, H.R.1
  • 3
    • 28244447739 scopus 로고    scopus 로고
    • GTPase activating proteins: Structural and functional insights 18 years after discovery
    • Scheffzek, K., and M. R. Ahmadian. 2005. GTPase activating proteins: structural and functional insights 18 years after discovery. Cell. Mol. Life Sci. 62:3014-3038.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 3014-3038
    • Scheffzek, K.1    Ahmadian, M.R.2
  • 4
    • 0035312395 scopus 로고    scopus 로고
    • GEFs: Master regulators of G-protein activation
    • Sprang, S. 2001. GEFs: master regulators of G-protein activation. Trends Biochem. Sci. 26:266-267.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 266-267
    • Sprang, S.1
  • 5
    • 0035282079 scopus 로고    scopus 로고
    • Substrate assisted catalysis-application to G proteins
    • Kosloff, M., and Z. Selinger. 2001. Substrate assisted catalysis-application to G proteins. Trends Biochem. Sci. 26:161-166.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 161-166
    • Kosloff, M.1    Selinger, Z.2
  • 7
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., P. Nissen, S. Thirup, and J. Nyborg. 1993. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1:35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 8
    • 0033081413 scopus 로고    scopus 로고
    • The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
    • Nissen, P., S. Thirup, M. Kjeldgaard, and J. Nyborg. 1999. The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Struct. Fold. Des. 7:143-156.
    • (1999) Struct. Fold. Des , vol.7 , pp. 143-156
    • Nissen, P.1    Thirup, S.2    Kjeldgaard, M.3    Nyborg, J.4
  • 9
    • 0028204451 scopus 로고
    • Solution structure and dynamics of Ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis, P. J., P. J. Domaille, S. L. Campbell-Burk, T. Van Aken, and E. D. Laue. 1994. Solution structure and dynamics of Ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 33:3515-3531.
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 10
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-Ras p21 at 1.35 A resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-Ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351-2359.
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 11
    • 0027132717 scopus 로고
    • The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S
    • Noel, J. P., H. E. Hamm, and P. B. Sigler. 1993. The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S. Nature. 366:654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 12
    • 0027965652 scopus 로고
    • Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
    • Coleman, D. E., A. M. Berghuis, E. Lee, M. E. Linder, A. G. Gilman, and S. R. Sprang. 1994. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Science. 265:1405-1412.
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 13
    • 13244277554 scopus 로고    scopus 로고
    • Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors
    • Leibundgut, M., C. Frick, M. Thanbichler, A. Bock, and N. Ban. 2005. Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors. EMBO J. 24:11-22.
    • (2005) EMBO J , vol.24 , pp. 11-22
    • Leibundgut, M.1    Frick, C.2    Thanbichler, M.3    Bock, A.4    Ban, N.5
  • 14
    • 1942470550 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe
    • Kong, C., K. Ito, M. A. Walsh, M. Wada, Y. Liu, S. Kumar, D. Barford, Y. Nakamura, and H. Song. 2004. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Mol. Cell. 14:233-245.
    • (2004) Mol. Cell , vol.14 , pp. 233-245
    • Kong, C.1    Ito, K.2    Walsh, M.A.3    Wada, M.4    Liu, Y.5    Kumar, S.6    Barford, D.7    Nakamura, Y.8    Song, H.9
  • 15
    • 1642304746 scopus 로고    scopus 로고
    • X-ray structure of translation initiation factor eIF2gamma
    • Roll Mecak, A., P. Alone, C. Cao, T. E. Dever, and K. S. Burley. 2003. X-ray structure of translation initiation factor eIF2gamma. J. Biol. Chem. 279:10634-10642.
    • (2003) J. Biol. Chem , vol.279 , pp. 10634-10642
    • Roll Mecak, A.1    Alone, P.2    Cao, C.3    Dever, T.E.4    Burley, K.S.5
  • 16
    • 23644451172 scopus 로고    scopus 로고
    • Crystal structure of a mutant elongation factor G trapped with a GTP analogue
    • Hansson, S., R. Singh, A. T. Gudkov, A. Liljas, and D. T. Logan. 2005. Crystal structure of a mutant elongation factor G trapped with a GTP analogue. FEBS Lett. 579:4492-4497.
    • (2005) FEBS Lett , vol.579 , pp. 4492-4497
    • Hansson, S.1    Singh, R.2    Gudkov, A.T.3    Liljas, A.4    Logan, D.T.5
  • 17
    • 0027733660 scopus 로고
    • GTPases. A turn-on and a surprise
    • Bourne, H. R. 1993. GTPases. A turn-on and a surprise. Nature. 366:628-629.
    • (1993) Nature , vol.366 , pp. 628-629
    • Bourne, H.R.1
  • 18
    • 0018089806 scopus 로고
    • The role of guanosine 59-triphosphate in polypeptide chain elongation
    • Kaziro, Y. 1978. The role of guanosine 59-triphosphate in polypeptide chain elongation. Biochim. Biophys. Acta. 505:95-127.
    • (1978) Biochim. Biophys. Acta , vol.505 , pp. 95-127
    • Kaziro, Y.1
  • 19
    • 0002498963 scopus 로고
    • Catalytic effects of elongation factor Ts on polypeptide synthesis
    • Ruusala, T., M. Ehrenberg, and C. G. Kurland. 1982. Catalytic effects of elongation factor Ts on polypeptide synthesis. EMBO J. 1:75-78.
    • (1982) EMBO J , vol.1 , pp. 75-78
    • Ruusala, T.1    Ehrenberg, M.2    Kurland, C.G.3
  • 20
    • 34247642630 scopus 로고    scopus 로고
    • Mechanism of EF-Ts-catalyzed guanine nucleotide exchange in EF-Tu: Contribution of interactions mediated by helix B of EF-Tu
    • Schummer, T., K. B. Gromadski, and M. V. Rodnina. 2007. Mechanism of EF-Ts-catalyzed guanine nucleotide exchange in EF-Tu: contribution of interactions mediated by helix B of EF-Tu. Biochemistry. 46:4977-4984.
    • (2007) Biochemistry , vol.46 , pp. 4977-4984
    • Schummer, T.1    Gromadski, K.B.2    Rodnina, M.V.3
  • 21
    • 0842267211 scopus 로고    scopus 로고
    • Kinetic determinants of high-fidelity tRNA discrimination on the ribosome
    • Gromadski, K. B., and M. V. Rodnina. 2004. Kinetic determinants of high-fidelity tRNA discrimination on the ribosome. Mol. Cell. 13:191-200.
    • (2004) Mol. Cell , vol.13 , pp. 191-200
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 22
    • 0037155195 scopus 로고    scopus 로고
    • Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base
    • Wieden, H. J., K. Gromadski, D. Rodnin, and M. V. Rodnina. 2002. Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base. J. Biol. Chem. 277:6032-6036.
    • (2002) J. Biol. Chem , vol.277 , pp. 6032-6036
    • Wieden, H.J.1    Gromadski, K.2    Rodnin, D.3    Rodnina, M.V.4
  • 23
    • 0033179296 scopus 로고    scopus 로고
    • GEFs: Structural basis for their activation of small GTP-binding proteins
    • Cherfils, J., and P. Chardin. 1999. GEFs: structural basis for their activation of small GTP-binding proteins. Trends Biochem. Sci. 24:306-311.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 306-311
    • Cherfils, J.1    Chardin, P.2
  • 24
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution
    • Kawashima, T., C. Berthet-Colominas, M. Wulff, S. Cusack, and R. Leberman. 1996. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Nature. 379:511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 26
    • 14244250065 scopus 로고    scopus 로고
    • Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex
    • Jeppesen, M. G., T. Navratil, L. L. Spremulli, and J. Nyborg. 2005. Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex. J. Biol. Chem. 280:5071-5081.
    • (2005) J. Biol. Chem , vol.280 , pp. 5071-5081
    • Jeppesen, M.G.1    Navratil, T.2    Spremulli, L.L.3    Nyborg, J.4
  • 27
    • 33745861301 scopus 로고    scopus 로고
    • Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha
    • Pittman, Y. R., L. Valente, M. G. Jeppesen, G. R. Andersen, S. Patel, and T. G. Kinzy. 2006. Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha. J. Biol. Chem. 281:19457-19468.
    • (2006) J. Biol. Chem , vol.281 , pp. 19457-19468
    • Pittman, Y.R.1    Valente, L.2    Jeppesen, M.G.3    Andersen, G.R.4    Patel, S.5    Kinzy, T.G.6
  • 28
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov, A. V., R. H. Buckingham, and M. Ehrenberg. 2001. A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell. 107:115-124.
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 29
    • 0035850833 scopus 로고    scopus 로고
    • High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts
    • Inoue, K., T. Maurer, H. Yamada, C. Herrmann, G. Horn, H. R. Kalbitzer, and K. Akasaka. 2001. High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts. FEBS Lett. 506:180-184.
    • (2001) FEBS Lett , vol.506 , pp. 180-184
    • Inoue, K.1    Maurer, T.2    Yamada, H.3    Herrmann, C.4    Horn, G.5    Kalbitzer, H.R.6    Akasaka, K.7
  • 30
    • 0034687081 scopus 로고    scopus 로고
    • Mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein
    • Hutchinson, J. P., and J. F. Eccleston. 2000. Mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein. Biochemistry. 39:11348-11359.
    • (2000) Biochemistry , vol.39 , pp. 11348-11359
    • Hutchinson, J.P.1    Eccleston, J.F.2
  • 31
    • 0034125425 scopus 로고    scopus 로고
    • Involvement of a small GTP-binding protein (G protein) regulator, small G protein GDP dissociation stimulator, in antiapoptotic cell survival signaling
    • Takakura, A., J. Miyoshi, H. Ishizaki, M. Tanaka, A. Togawa, Y. Nishizawa, H. Yoshida, S. Nishikawa, and Y. Takai. 2000. Involvement of a small GTP-binding protein (G protein) regulator, small G protein GDP dissociation stimulator, in antiapoptotic cell survival signaling. Mol. Biol. Cell. 11:1875-1886.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1875-1886
    • Takakura, A.1    Miyoshi, J.2    Ishizaki, H.3    Tanaka, M.4    Togawa, A.5    Nishizawa, Y.6    Yoshida, H.7    Nishikawa, S.8    Takai, Y.9
  • 32
    • 0018156514 scopus 로고
    • Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. 2. Catalytic properties
    • Arai, K., N. Arai, S. Nakamura, T. Oshima, and Y. Kaziro. 1978. Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8. 2. Catalytic properties. Eur. J. Biochem. 92:521-531.
    • (1978) Eur. J. Biochem , vol.92 , pp. 521-531
    • Arai, K.1    Arai, N.2    Nakamura, S.3    Oshima, T.4    Kaziro, Y.5
  • 33
    • 0037039281 scopus 로고    scopus 로고
    • Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu
    • Gromadski, K. B., H. J. Wieden, and M. V. Rodnina. 2002. Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu. Biochemistry. 41:162-169.
    • (2002) Biochemistry , vol.41 , pp. 162-169
    • Gromadski, K.B.1    Wieden, H.J.2    Rodnina, M.V.3
  • 35
    • 33746728252 scopus 로고    scopus 로고
    • Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3
    • Hauryliuk, V., A. Zavialov, L. Kisselev, and M. Ehrenberg. 2006. Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3. Biochimie. 88:747-757.
    • (2006) Biochimie , vol.88 , pp. 747-757
    • Hauryliuk, V.1    Zavialov, A.2    Kisselev, L.3    Ehrenberg, M.4
  • 36
    • 33748572261 scopus 로고    scopus 로고
    • Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct
    • Mitkevich, V. A., A. V. Kononenko, I. Y. Petrushanko, D. V. Yanvarev, A. A. Makarov, and L. L. Kisselev. 2006. Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct. Nucleic Acids Res. 34:3947-3954.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3947-3954
    • Mitkevich, V.A.1    Kononenko, A.V.2    Petrushanko, I.Y.3    Yanvarev, D.V.4    Makarov, A.A.5    Kisselev, L.L.6
  • 37
    • 33845992204 scopus 로고    scopus 로고
    • Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides
    • Pisareva, V. P., A. V. Pisarev, C. U. Hellen, M. V. Rodnina, and T. V. Pestova. 2006. Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides. J. Biol. Chem. 281:40224-40235.
    • (2006) J. Biol. Chem , vol.281 , pp. 40224-40235
    • Pisareva, V.P.1    Pisarev, A.V.2    Hellen, C.U.3    Rodnina, M.V.4    Pestova, T.V.5
  • 38
    • 20444393817 scopus 로고    scopus 로고
    • Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs
    • Zavialov, A. V., V. V. Hauryliuk, and M. Ehrenberg. 2005. Guanine-nucleotide exchange on ribosome-bound elongation factor G initiates the translocation of tRNAs. J. Biol. 4:1-9.
    • (2005) J. Biol , vol.4 , pp. 1-9
    • Zavialov, A.V.1    Hauryliuk, V.V.2    Ehrenberg, M.3
  • 39
    • 0017160838 scopus 로고
    • Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome
    • Baca, O. G., M. S. Rohrbach, and J. W. Bodley. 1976. Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome. Biochemistry. 15:4570-4574.
    • (1976) Biochemistry , vol.15 , pp. 4570-4574
    • Baca, O.G.1    Rohrbach, M.S.2    Bodley, J.W.3
  • 41
    • 0034607684 scopus 로고    scopus 로고
    • Effectors increase the affinity of ADP-ribosylation factor for GTP to increase binding
    • Zhu, X., A. L. Boman, J. Kuai, W. Cieplak, and R. A. Kahn. 2000. Effectors increase the affinity of ADP-ribosylation factor for GTP to increase binding. J. Biol. Chem. 275:13465-13475.
    • (2000) J. Biol. Chem , vol.275 , pp. 13465-13475
    • Zhu, X.1    Boman, A.L.2    Kuai, J.3    Cieplak, W.4    Kahn, R.A.5
  • 43
    • 0015411506 scopus 로고    scopus 로고
    • Kaziro, Y., N. Inoue-Yokosawa, and M. Kawakita. 1972. Studies on polypeptide elongation factor from E. coli. I. Crystalline factor G. J. Biochem. (Tokyo). 72:853-863.
    • Kaziro, Y., N. Inoue-Yokosawa, and M. Kawakita. 1972. Studies on polypeptide elongation factor from E. coli. I. Crystalline factor G. J. Biochem. (Tokyo). 72:853-863.
  • 45
    • 0025098898 scopus 로고
    • Effects of nucleotide- and aurodox-induced changes in elongation factor Tu conformation upon its interactions with aminoacyl transfer RNA. A fluorescence study
    • Dell, V. A., D. L. Miller, and A. E. Johnson. 1990. Effects of nucleotide- and aurodox-induced changes in elongation factor Tu conformation upon its interactions with aminoacyl transfer RNA. A fluorescence study. Biochemistry. 29:1757-1763.
    • (1990) Biochemistry , vol.29 , pp. 1757-1763
    • Dell, V.A.1    Miller, D.L.2    Johnson, A.E.3
  • 46
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. 2002. Ribosome structure and the mechanism of translation. Cell. 108:557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 47
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution
    • Czworkowski, J., J. Wang, T. A. Steitz, and P. B. Moore. 1994. The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution. EMBO J. 13:3661-3668.
    • (1994) EMBO J , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 49
    • 0030585061 scopus 로고    scopus 로고
    • The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange
    • al-Karadaghi, S., A. Aevarsson, M. Garber, J. Zheltonosova, and A. Liljas. 1996. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure. 4:555-565.
    • (1996) Structure , vol.4 , pp. 555-565
    • al-Karadaghi, S.1    Aevarsson, A.2    Garber, M.3    Zheltonosova, J.4    Liljas, A.5
  • 50
    • 33748785471 scopus 로고    scopus 로고
    • Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome
    • Wilden, B., A. Savelsbergh, M. V. Rodnina, and W. Wintermeyer. 2006. Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome. Proc. Natl. Acad. Sci. USA. 103:13670-13675.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13670-13675
    • Wilden, B.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 51
    • 0242516080 scopus 로고    scopus 로고
    • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
    • Jorgensen, R., P. A. Ortiz, A. Carr-Schmid, P. Nissen, T. G. Kinzy, and G. R. Andersen. 2003. Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Nat. Struct. Biol. 10:379-385.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 379-385
    • Jorgensen, R.1    Ortiz, P.A.2    Carr-Schmid, A.3    Nissen, P.4    Kinzy, T.G.5    Andersen, G.R.6
  • 53
    • 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., C. Cao, T. E. Dever, and S. K. Burley. 2000. X-ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding. Cell. 103:781-792.
    • (2000) Cell , vol.103 , pp. 781-792
    • Roll-Mecak, A.1    Cao, C.2    Dever, T.E.3    Burley, S.K.4
  • 54
    • 0037007203 scopus 로고    scopus 로고
    • The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
    • Schmitt, E., S. Blanquet, and Y. Mechulam. 2002. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21:1821-1832.
    • (2002) EMBO J , vol.21 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 55
    • 0030850032 scopus 로고    scopus 로고
    • The conformational properties of elongation factor G and the mechanism of translocation
    • Czworkowski, J., and P. B. Moore. 1997. The conformational properties of elongation factor G and the mechanism of translocation. Biochemistry. 36:10327-10334.
    • (1997) Biochemistry , vol.36 , pp. 10327-10334
    • Czworkowski, J.1    Moore, P.B.2
  • 56
    • 0016699039 scopus 로고
    • Formation of a binary complex between elongation factor G and guanine nucleotides
    • Arai, N., K. Arai, and Y. Kaziro. 1975. Formation of a binary complex between elongation factor G and guanine nucleotides. J. Biochem. (Tokyo). 78:243-246.
    • (1975) J. Biochem. (Tokyo) , vol.78 , pp. 243-246
    • Arai, N.1    Arai, K.2    Kaziro, Y.3
  • 57
    • 33748350921 scopus 로고    scopus 로고
    • Structure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 region
    • Sokabe, M., M. Yao, N. Sakai, S. Toya, and I. Tanaka. 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.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13016-13021
    • Sokabe, M.1    Yao, M.2    Sakai, N.3    Toya, S.4    Tanaka, I.5
  • 58
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer
    • Yatime, L., Y. Mechulam, S. Blanquet, and E. Schmitt. 2006. Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer. Structure. 14:119-128.
    • (2006) Structure , vol.14 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 59
    • 0035907234 scopus 로고    scopus 로고
    • Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox
    • Vogeley, L., G. J. Palm, J. R. Mesters, and R. Hilgenfeld. 2001. Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox. J. Biol. Chem. 276:17149-17155.
    • (2001) J. Biol. Chem , vol.276 , pp. 17149-17155
    • Vogeley, L.1    Palm, G.J.2    Mesters, J.R.3    Hilgenfeld, R.4
  • 60
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D. D., Y. I. Wolf, E. V. Koonin, and L. Aravind. 2002. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317:41-72.
    • (2002) J. Mol. Biol , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 63
    • 0038300651 scopus 로고    scopus 로고
    • Peptidyl-tRNA regulates the GTPase activity of translation factors
    • Zavialov, A. V., and M. Ehrenberg. 2003. Peptidyl-tRNA regulates the GTPase activity of translation factors. Cell. 114:113-122.
    • (2003) Cell , vol.114 , pp. 113-122
    • Zavialov, A.V.1    Ehrenberg, M.2
  • 64
    • 0035787732 scopus 로고    scopus 로고
    • Ratchet-like movements between the two ribosomal subunits: Their implications in elongation factor recognition and tRNA translocation
    • Frank, J., and R. K. Agrawal. 2001. Ratchet-like movements between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation. Cold Spring Harb. Symp. Quant. Biol. 66:67-75.
    • (2001) Cold Spring Harb. Symp. Quant. Biol , vol.66 , pp. 67-75
    • Frank, J.1    Agrawal, R.K.2
  • 65
    • 25644436944 scopus 로고    scopus 로고
    • Translation initiation: Structures, mechanisms and evolution
    • Marintchev, A., and G. Wagner. 2004. Translation initiation: structures, mechanisms and evolution. Q. Rev. Biophys. 37:197-284.
    • (2004) Q. Rev. Biophys , vol.37 , pp. 197-284
    • Marintchev, A.1    Wagner, G.2
  • 66
    • 0023928418 scopus 로고
    • Kinetic studies on the role of elongation factors 1 beta and 1 gamma in protein synthesis
    • Janssen, G. M., and W. Moller. 1988. Kinetic studies on the role of elongation factors 1 beta and 1 gamma in protein synthesis. J. Biol. Chem. 263:1773-1778.
    • (1988) J. Biol. Chem , vol.263 , pp. 1773-1778
    • Janssen, G.M.1    Moller, W.2
  • 67
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha
    • Andersen, G. R., L. Pedersen, L. Valente, I. Chatterjee, T. G. Kinzy, M. Kjeldgaard, and J. Nyborg. 2000. Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Mol. Cell. 6:1261-1266.
    • (2000) Mol. Cell , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 68
    • 0035816596 scopus 로고    scopus 로고
    • Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein
    • Williams, D. D., N. T. Price, A. J. Loughlin, and C. G. Proud. 2001. Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein. J. Biol. Chem. 276:24697-24703.
    • (2001) J. Biol. Chem , vol.276 , pp. 24697-24703
    • Williams, D.D.1    Price, N.T.2    Loughlin, A.J.3    Proud, C.G.4
  • 69
    • 29244445859 scopus 로고    scopus 로고
    • Control of phosphate release from elongation factor G by ribosomal protein L7/12
    • Savelsbergh, A., D. Mohr, U. Kothe, W. Wintermeyer, and M. V. Rodnina. 2005. Control of phosphate release from elongation factor G by ribosomal protein L7/12. EMBO J. 24:4316-4323.
    • (2005) EMBO J , vol.24 , pp. 4316-4323
    • Savelsbergh, A.1    Mohr, D.2    Kothe, U.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 70
    • 26944435515 scopus 로고    scopus 로고
    • Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • Algire, M. A., D. Maag, and J. R. Lorsch. 2005. 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) Mol. Cell , vol.20 , pp. 251-262
    • Algire, M.A.1    Maag, D.2    Lorsch, J.R.3
  • 71
    • 33749014394 scopus 로고    scopus 로고
    • A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein
    • Kotting, C., M. Blessenohl, Y. Suveyzdis, R. S. Goody, A. Wittinghofer, and K. Gerwert. 2006. A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein. Proc. Natl. Acad. Sci. USA. 103:13911-13916.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13911-13916
    • Kotting, C.1    Blessenohl, M.2    Suveyzdis, Y.3    Goody, R.S.4    Wittinghofer, A.5    Gerwert, K.6
  • 72
    • 0037184985 scopus 로고    scopus 로고
    • Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
    • Shin, B. S., D. Maag, A. Roll-Mecak, M. S. Arefin, S. K. Burley, J. R. Lorsch, and T. E. Dever. 2002. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell. 111:1015-1025.
    • (2002) Cell , vol.111 , pp. 1015-1025
    • Shin, B.S.1    Maag, D.2    Roll-Mecak, A.3    Arefin, M.S.4    Burley, S.K.5    Lorsch, J.R.6    Dever, T.E.7
  • 74
    • 0021751219 scopus 로고
    • Guanosine nucleotide binding by highly purified Ha-ras-encoded p21 protein produced in Escherichia coli
    • Manne, V., S. Yamazaki, and H. F. Kung. 1984. Guanosine nucleotide binding by highly purified Ha-ras-encoded p21 protein produced in Escherichia coli. Proc. Natl. Acad. Sci. USA. 81:6953-6957.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6953-6957
    • Manne, V.1    Yamazaki, S.2    Kung, H.F.3
  • 75
    • 0030577375 scopus 로고    scopus 로고
    • Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin
    • Kristensen, O., L. Reshetnikova, P. Nissen, G. Siboska, S. Thirup, and J. Nyborg. 1996. Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin. FEBS Lett. 399:59-62.
    • (1996) FEBS Lett , vol.399 , pp. 59-62
    • Kristensen, O.1    Reshetnikova, L.2    Nissen, P.3    Siboska, G.4    Thirup, S.5    Nyborg, J.6
  • 76
    • 0023655668 scopus 로고
    • Purification and characterization of Saccharomyces cerevisiae mitochondrial elongation factor Tu
    • Rosenthal, L. P., and J. W. Bodley. 1987. Purification and characterization of Saccharomyces cerevisiae mitochondrial elongation factor Tu. J. Biol. Chem. 262:10955-10959.
    • (1987) J. Biol. Chem , vol.262 , pp. 10955-10959
    • Rosenthal, L.P.1    Bodley, J.W.2
  • 77
    • 0039765528 scopus 로고    scopus 로고
    • Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA
    • Thanbichler, M., A. Bock, and R. S. Goody. 2000. Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA. J. Biol. Chem. 275:20458-20466.
    • (2000) J. Biol. Chem , vol.275 , pp. 20458-20466
    • Thanbichler, M.1    Bock, A.2    Goody, R.S.3
  • 78
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen, G. S., A. Zavialov, R. Gursky, M. Ehrenberg, and J. Frank. 2005. The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell. 121:703-712.
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 79
    • 33947211185 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of guanine nucleotides with eukaryotic translation initiation factor eIF5B
    • Pisareva, V. P., C. U. Hellen, and T. V. Pestova. 2007. Kinetic analysis of the interaction of guanine nucleotides with eukaryotic translation initiation factor eIF5B. Biochemistry. 46:2622-2629.
    • (2007) Biochemistry , vol.46 , pp. 2622-2629
    • Pisareva, V.P.1    Hellen, C.U.2    Pestova, T.V.3
  • 80
    • 0021826803 scopus 로고
    • Structure-function relationship in Escherichia coli initiation factors. Biochemical and biophysical characterization of the interaction between IF-2 and guanosine nucleotides
    • Pon, C. L., M. Paci, R. T. Pawlik, and C.O. Gualerzi. 1985. Structure-function relationship in Escherichia coli initiation factors. Biochemical and biophysical characterization of the interaction between IF-2 and guanosine nucleotides. J Biol. Chem. 260:8918-8924.
    • (1985) J Biol. Chem , vol.260 , pp. 8918-8924
    • Pon, C.L.1    Paci, M.2    Pawlik, R.T.3    Gualerzi, C.O.4
  • 81
    • 0037007203 scopus 로고    scopus 로고
    • The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
    • Schmitt, E., S. Blanquet, and Y. Mechulam. 2002. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21:1821-1832.
    • (2002) EMBO J , vol.21 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 82
    • 15944425052 scopus 로고    scopus 로고
    • The archaeal eIF2 homologue: Functional properties of an ancient translation initiation factor
    • Pedulla, N., R. Palermo, D. Hasenohrl, U. Blasi, P. Cammarano, and P. Londei. 2005. The archaeal eIF2 homologue: functional properties of an ancient translation initiation factor. Nucleic Acids Res. 33:1804-1812.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1804-1812
    • Pedulla, N.1    Palermo, R.2    Hasenohrl, D.3    Blasi, U.4    Cammarano, P.5    Londei, P.6
  • 83
    • 0023654065 scopus 로고
    • Purification and characterization of eukaryotic initiation factor 2 and a guanine nucleotide exchange factor from rat liver
    • Kimball, S. R., W. V. Everson, L. M. Myers, and L. S. Jefferson. 1987. Purification and characterization of eukaryotic initiation factor 2 and a guanine nucleotide exchange factor from rat liver. J. Biol. Chem. 262:2220-2227.
    • (1987) J. Biol. Chem , vol.262 , pp. 2220-2227
    • Kimball, S.R.1    Everson, W.V.2    Myers, L.M.3    Jefferson, L.S.4
  • 84
    • 0035816596 scopus 로고    scopus 로고
    • Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein
    • Williams, D. D., N. T. Price, A. J. Loughlin, and C. G. Proud. 2001. Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein. J. Biol. Chem. 276:24697-24703.
    • (2001) J. Biol. Chem , vol.276 , pp. 24697-24703
    • Williams, D.D.1    Price, N.T.2    Loughlin, A.J.3    Proud, C.G.4


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