메뉴 건너뛰기




Volumn 332, Issue 3, 2003, Pages 689-699

Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome

Author keywords

GTP binding proteins; Rapid kinetics; Stopped flow; Translation

Indexed keywords

ELONGATION FACTOR TU; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; HISTIDINE 84; HISTIDINE DERIVATIVE; UNCLASSIFIED DRUG; WATER;

EID: 0041735420     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00947-1     Document Type: Article
Times cited : (127)

References (42)
  • 1
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai E.F., Krengel U., Petsko G.A., Goody R.S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1. 35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:1990;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
  • 3
    • 0028464366 scopus 로고
    • Why have mutagenesis studies not located the general base in ras p21
    • Schweins T., Langen R., Warshel A. Why have mutagenesis studies not located the general base in ras p21. Nature Struct. Biol. 1:1994;476-484.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 476-484
    • Schweins, T.1    Langen, R.2    Warshel, A.3
  • 4
    • 0029843561 scopus 로고    scopus 로고
    • Mechanistic analysis of the observed linear free energy relationships in p21ras and related systems
    • Schweins T., Warshel A. Mechanistic analysis of the observed linear free energy relationships in p21ras and related systems. Biochemistry. 35:1996;14232-14243.
    • (1996) Biochemistry , vol.35 , pp. 14232-14243
    • Schweins, T.1    Warshel, A.2
  • 6
    • 0029825324 scopus 로고    scopus 로고
    • Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5′-triphosphate hydrolysis of p21ras
    • Schweins T., Geyer M., Kalbitzer H.R., Wittinghofer A., Warshel A. Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5′-triphosphate hydrolysis of p21ras. Biochemistry. 35:1996;14225-14231.
    • (1996) Biochemistry , vol.35 , pp. 14225-14231
    • Schweins, T.1    Geyer, M.2    Kalbitzer, H.R.3    Wittinghofer, A.4    Warshel, A.5
  • 7
    • 0033511228 scopus 로고    scopus 로고
    • Nucleoside triphosphate-binding proteins: Different scaffolds to achieve phosphoryl transfer
    • Vetter I.R., Wittinghofer A. Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer. Quart. Rev. Biophys. 32:1999;1-56.
    • (1999) Quart. Rev. Biophys. , vol.32 , pp. 1-56
    • Vetter, I.R.1    Wittinghofer, A.2
  • 8
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:1991;117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 10
    • 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., Palm G.J., Mesters J.R., Hilgenfeld R. 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. 276:2001;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
  • 11
    • 0021781999 scopus 로고
    • Mechanism of action of kirromycin-like antibiotics
    • Parmeggiani A., Swart G.W. Mechanism of action of kirromycin-like antibiotics. Annu. Rev. Microbiol. 39:1985;557-577.
    • (1985) Annu. Rev. Microbiol. , vol.39 , pp. 557-577
    • Parmeggiani, A.1    Swart, G.W.2
  • 12
    • 0032535207 scopus 로고    scopus 로고
    • Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome
    • Pape T., Wintermeyer W., Rodnina M.V. Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J. 17:1998;7490-7497.
    • (1998) EMBO J. , vol.17 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 13
    • 0032878323 scopus 로고    scopus 로고
    • Mutagenesis of three residues, isoleucine-60, threonine-61, and aspartic acid-80, implicated in the GTPase activity of Escherichia coli elongation factor Tu
    • Krab I.M., Parmeggiani A. Mutagenesis of three residues, isoleucine-60, threonine-61, and aspartic acid-80, implicated in the GTPase activity of Escherichia coli elongation factor Tu. Biochemistry. 38:1999;13035-13041.
    • (1999) Biochemistry , vol.38 , pp. 13035-13041
    • Krab, I.M.1    Parmeggiani, A.2
  • 14
    • 0026065669 scopus 로고
    • Substitution of histidine-84 and the GTPase mechanism of elongation factor Tu
    • Cool R.H., Parmeggiani A. Substitution of histidine-84 and the GTPase mechanism of elongation factor Tu. Biochemistry. 30:1991;362-366.
    • (1991) Biochemistry , vol.30 , pp. 362-366
    • Cool, R.H.1    Parmeggiani, A.2
  • 15
    • 0029061952 scopus 로고
    • Relevance of histidine-84 in the elongation factor Tu GTPase activity and in poly(Phe) synthesis: Its substitution by glutamine and alanine
    • Scarano G., Krab I.M., Bocchini V., Parmeggiani A. Relevance of histidine-84 in the elongation factor Tu GTPase activity and in poly(Phe) synthesis: its substitution by glutamine and alanine. FEBS Letters. 365:1995;214-218.
    • (1995) FEBS Letters , vol.365 , pp. 214-218
    • Scarano, G.1    Krab, I.M.2    Bocchini, V.3    Parmeggiani, A.4
  • 16
    • 0028937947 scopus 로고
    • Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300
    • Zeidler W., Egle C., Ribeiro S., Wagner A., Katunin V., Kreutzer R., et al. Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300. Eur. J. Biochem. 229:1995;596-604.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 596-604
    • Zeidler, W.1    Egle, C.2    Ribeiro, S.3    Wagner, A.4    Katunin, V.5    Kreutzer, R.6
  • 17
    • 0028109919 scopus 로고
    • Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu
    • Rodnina M.V., Fricke R., Wintermeyer W. Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu. Biochemistry. 33:1994;12267-12275.
    • (1994) Biochemistry , vol.33 , pp. 12267-12275
    • Rodnina, M.V.1    Fricke, R.2    Wintermeyer, W.3
  • 18
    • 0035933781 scopus 로고    scopus 로고
    • The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome
    • Knudsen C., Wieden H.J., Rodnina M.V. The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome. J. Biol. Chem. 276:2001;22183-22190.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22183-22190
    • Knudsen, C.1    Wieden, H.J.2    Rodnina, M.V.3
  • 19
    • 0030047916 scopus 로고    scopus 로고
    • Initial binding of the elongation factor Tu·GTP· aminoacyl-tRNA complex preceding codon recognition on the ribosome
    • Rodnina M.V., Pape T., Fricke R., Kuhn L., Wintermeyer W. Initial binding of the elongation factor Tu·GTP·aminoacyl-tRNA complex preceding codon recognition on the ribosome. J. Biol. Chem. 271:1996;646-652.
    • (1996) J. Biol. Chem. , vol.271 , pp. 646-652
    • Rodnina, M.V.1    Pape, T.2    Fricke, R.3    Kuhn, L.4    Wintermeyer, W.5
  • 20
    • 0029006133 scopus 로고
    • Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome
    • Rodnina M.V., Fricke R., Kuhn L., Wintermeyer W. Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome. EMBO J. 14:1995;2613-2619.
    • (1995) EMBO J. , vol.14 , pp. 2613-2619
    • Rodnina, M.V.1    Fricke, R.2    Kuhn, L.3    Wintermeyer, W.4
  • 22
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape T., Wintermeyer W., Rodnina M.V. Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 18:1999;3800-3807.
    • (1999) EMBO J. , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 23
    • 0023977682 scopus 로고
    • EFTu provides an internal kinetic standard for translational accuracy
    • Thompson R.C. EFTu provides an internal kinetic standard for translational accuracy. Trends Biochem. Sci. 13:1988;91-93.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 91-93
    • Thompson, R.C.1
  • 24
    • 0037039281 scopus 로고    scopus 로고
    • Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu
    • Gromadski K.B., Wieden H.J., Rodnina M.V. Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu. Biochemistry. 41:2002;162-169.
    • (2002) Biochemistry , vol.41 , pp. 162-169
    • Gromadski, K.B.1    Wieden, H.J.2    Rodnina, M.V.3
  • 25
    • 0016734139 scopus 로고
    • Partition analysis and the concept of net rate constants as tools in enzyme kinetics
    • Cleland W.W. Partition analysis and the concept of net rate constants as tools in enzyme kinetics. Biochemistry. 14:1975;3220-3224.
    • (1975) Biochemistry , vol.14 , pp. 3220-3224
    • Cleland, W.W.1
  • 26
    • 0022974685 scopus 로고
    • Guanosine 5′-O-(3-thiotriphosphate) as an analog of GTP in protein biosynthesis. The effects of temperature and polycations on the accuracy of initial recognition of aminoacyl-tRNA ternary complexes by ribosomes
    • Karim A.M., Thompson R.C. Guanosine 5′-O-(3-thiotriphosphate) as an analog of GTP in protein biosynthesis. The effects of temperature and polycations on the accuracy of initial recognition of aminoacyl-tRNA ternary complexes by ribosomes. J. Biol. Chem. 261:1986;3238-3243.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3238-3243
    • Karim, A.M.1    Thompson, R.C.2
  • 27
    • 0030600518 scopus 로고    scopus 로고
    • Dynamics and morphology of the in vitro polymeric form of elongation factor Tu from Escherichia coli
    • Helms M.K., Marriott G., Sawyer W.H., Jameson D.M. Dynamics and morphology of the in vitro polymeric form of elongation factor Tu from Escherichia coli. Biochim. Biophys. Acta. 1291:1996;122-130.
    • (1996) Biochim. Biophys. Acta , vol.1291 , pp. 122-130
    • Helms, M.K.1    Marriott, G.2    Sawyer, W.H.3    Jameson, D.M.4
  • 28
    • 0029402275 scopus 로고
    • Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: Mechanism and GTP consumption
    • Rodnina M.V., Pape T., Fricke R., Wintermeyer W. Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption. Biochem. Cell Biol. 73:1995;1221-1227.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 1221-1227
    • Rodnina, M.V.1    Pape, T.2    Fricke, R.3    Wintermeyer, W.4
  • 29
    • 0029548957 scopus 로고
    • Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: Effects on the GTPase reaction and aminoacyl-tRNA binding
    • Knudsen C.R., Clark B.F. Site-directed mutagenesis of Arg58 and Asp86 of elongation factor Tu from Escherichia coli: effects on the GTPase reaction and aminoacyl-tRNA binding. Protein Eng. 8:1995;1267-1273.
    • (1995) Protein Eng. , vol.8 , pp. 1267-1273
    • Knudsen, C.R.1    Clark, B.F.2
  • 30
    • 0030727501 scopus 로고    scopus 로고
    • Mutational analysis of Escherichia coli elongation factor Tu in search of a role for the N-terminal region
    • Mansilla F., Knudsen C.R., Laurberg M., Clark B.F. Mutational analysis of Escherichia coli elongation factor Tu in search of a role for the N-terminal region. Protein Eng. 10:1997;927-934.
    • (1997) Protein Eng. , vol.10 , pp. 927-934
    • Mansilla, F.1    Knudsen, C.R.2    Laurberg, M.3    Clark, B.F.4
  • 31
    • 0030669758 scopus 로고    scopus 로고
    • Contribution of Arg288 of Escherichia coli elongation factor Tu to translational functionality
    • Rattenborg T., Nautrup Pedersen G., Clark B.F., Knudsen C.R. Contribution of Arg288 of Escherichia coli elongation factor Tu to translational functionality. Eur. J. Biochem. 249:1997;408-414.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 408-414
    • Rattenborg, T.1    Nautrup Pedersen, G.2    Clark, B.F.3    Knudsen, C.R.4
  • 32
    • 0029786512 scopus 로고    scopus 로고
    • Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA
    • Wiborg O., Andersen C., Knudsen C.R., Clark B.F., Nyborg J. Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. J. Biol. Chem. 271:1996;20406-20411.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20406-20411
    • Wiborg, O.1    Andersen, C.2    Knudsen, C.R.3    Clark, B.F.4    Nyborg, J.5
  • 36
    • 0000149854 scopus 로고    scopus 로고
    • Mechanisms of partial reactions of the elongation cycle catalyzed by elongation factors Tu and G
    • R.A. Garrett, S.R. Douthwaite, A. Liljas, A.T. Matheson, P.B. Moore, & H.F. Noller. Washington, DC: ASM Press
    • Rodnina M.V., Pape T., Savelsbergh A., Mohr D., Matassova N.B., Wintermeyer W. Mechanisms of partial reactions of the elongation cycle catalyzed by elongation factors Tu and G. Garrett R.A., Douthwaite S.R., Liljas A., Matheson A.T., Moore P.B., Noller H.F. The Ribosome: Structure, Functiom, Antibiotics, and Cellular Interactions. 2000;301-317 ASM Press, Washington, DC.
    • (2000) The Ribosome: Structure, Functiom, Antibiotics, and Cellular Interactions , pp. 301-317
    • Rodnina, M.V.1    Pape, T.2    Savelsbergh, A.3    Mohr, D.4    Matassova, N.B.5    Wintermeyer, W.6
  • 37
    • 0037108102 scopus 로고    scopus 로고
    • GTPase activation of elongation factors Tu and G on the ribosome
    • Mohr D., Wintermeyer W., Rodnina M.V. GTPase activation of elongation factors Tu and G on the ribosome. Biochemistry. 41:2002;12520-12528.
    • (2002) Biochemistry , vol.41 , pp. 12520-12528
    • Mohr, D.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 38
    • 0034700993 scopus 로고    scopus 로고
    • Intact aminoacyl-tRNA is required to trigger GTP hydrolysis by elongation factor Tu on the ribosome
    • Piepenburg O., Pape T., Pleiss J.A., Wintermeyer W., Uhlenbeck O., Rodnina M.V. Intact aminoacyl-tRNA is required to trigger GTP hydrolysis by elongation factor Tu on the ribosome. Biochemistry. 39:2000;1734-1738.
    • (2000) Biochemistry , vol.39 , pp. 1734-1738
    • Piepenburg, O.1    Pape, T.2    Pleiss, J.A.3    Wintermeyer, W.4    Uhlenbeck, O.5    Rodnina, M.V.6
  • 39
    • 0028941626 scopus 로고
    • GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs
    • Rodnina M.V., Wintermeyer W. GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs. Proc. Natl Acad. Sci. USA. 92:1995;1945-1949.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1945-1949
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 40
    • 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., Gromadski K., Rodnin D., Rodnina M.V. Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base. J. Biol. Chem. 277:2002;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
  • 41
    • 0019520976 scopus 로고
    • The identification and analysis of nucleotides bound to the elongation factor Tu from Escherichia coli
    • Block W., Pingoud A. The identification and analysis of nucleotides bound to the elongation factor Tu from Escherichia coli. Anal. Biochem. 114:1981;112-117.
    • (1981) Anal. Biochem. , vol.114 , pp. 112-117
    • Block, W.1    Pingoud, A.2
  • 42
    • 0026521547 scopus 로고
    • Kinetic properties of Escherichia coli ribosomes with altered forms of S12
    • Bilgin N., Claesens F., Pahverk H., Ehrenberg M. Kinetic properties of Escherichia coli ribosomes with altered forms of S12. J. Mol. Biol. 224:1992;1011-1027.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1011-1027
    • Bilgin, N.1    Claesens, F.2    Pahverk, H.3    Ehrenberg, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.