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Volumn 54, Issue 2, 2015, Pages 363-376

Steady-state kinetics and spectroscopic characterization of enzyme-tRNA interactions for the non-heme diiron tRNA-monooxygenase, MiaE

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; CATALYSIS; DICHROISM; DYES; ELECTRON TRANSPORT PROPERTIES; ELECTRONIC STRUCTURE; ENZYMES; HYDROXYLATION; MAGNETIC RESONANCE; PARAMAGNETIC RESONANCE; PORPHYRINS; PROTEINS; SALMONELLA;

EID: 84922463660     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5012207     Document Type: Article
Times cited : (10)

References (64)
  • 4
    • 0027245490 scopus 로고
    • Modification of tRNA as a regulatory device
    • Persson, B. C. (1993) Modification of tRNA as a regulatory device Mol. Microbiol. 8, 1011-1016
    • (1993) Mol. Microbiol. , vol.8 , pp. 1011-1016
    • Persson, B.C.1
  • 5
    • 22244433549 scopus 로고    scopus 로고
    • Antibiotics Targeting Ribosomes: Resistance, Selectivity, Synergism, and Cellular Regulation
    • Yonath, A. (2005) Antibiotics Targeting Ribosomes: Resistance, Selectivity, Synergism, and Cellular Regulation Annu. Rev. Biochem. 74, 649-679
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 649-679
    • Yonath, A.1
  • 6
    • 43049130865 scopus 로고    scopus 로고
    • HIV-1 reverse transcription initiation: A potential target for novel antivirals?
    • Abbink, T. E. M. and Berkhout, B. (2008) HIV-1 reverse transcription initiation: A potential target for novel antivirals? Virus Res. 134, 4-18
    • (2008) Virus Res. , vol.134 , pp. 4-18
    • Abbink, T.E.M.1    Berkhout, B.2
  • 7
    • 84878696881 scopus 로고    scopus 로고
    • MiRNA: The new frontier in cancer medicine
    • Ju, J., Jiang, J., and Fesler, A. (2013) miRNA: The new frontier in cancer medicine Future Med. Chem. 5, 983-985
    • (2013) Future Med. Chem. , vol.5 , pp. 983-985
    • Ju, J.1    Jiang, J.2    Fesler, A.3
  • 11
    • 0031019672 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme
    • Moore, J. A. and Poulter, C. D. (1997) Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme Biochemistry 36, 604-614
    • (1997) Biochemistry , vol.36 , pp. 604-614
    • Moore, J.A.1    Poulter, C.D.2
  • 13
    • 9144220291 scopus 로고    scopus 로고
    • MiaB Protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA
    • Pierrel, F., Douki, T., Fontecave, M., and Atta, M. (2004) MiaB Protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA J. Biol. Chem. 279, 47555-47563
    • (2004) J. Biol. Chem. , vol.279 , pp. 47555-47563
    • Pierrel, F.1    Douki, T.2    Fontecave, M.3    Atta, M.4
  • 14
    • 77956514978 scopus 로고    scopus 로고
    • Identification of Eukaryotic and Prokaryotic Methylthiotransferase for Biosynthesis of 2-Methylthio-N6-threonylcarbamoyladenosine in tRNA
    • Arragain, S., Handelman, S. K., Forouhar, F., Wei, F.-Y., Tomizawa, K., Hunt, J. F., Douki, T., Fontecave, M., Mulliez, E., and Atta, M. (2010) Identification of Eukaryotic and Prokaryotic Methylthiotransferase for Biosynthesis of 2-Methylthio-N6-threonylcarbamoyladenosine in tRNA J. Biol. Chem. 285, 28425-28433
    • (2010) J. Biol. Chem. , vol.285 , pp. 28425-28433
    • Arragain, S.1    Handelman, S.K.2    Forouhar, F.3    Wei, F.-Y.4    Tomizawa, K.5    Hunt, J.F.6    Douki, T.7    Fontecave, M.8    Mulliez, E.9    Atta, M.10
  • 18
    • 0021256993 scopus 로고
    • A modified nucleotide in tRNA as a possible regulator of aerobiosis: Synthesis of cis-2-methyl-thioribosylzeatin in the tRNA of Salmonella
    • Buck, M. and Ames, B. N. (1984) A modified nucleotide in tRNA as a possible regulator of aerobiosis: Synthesis of cis-2-methyl-thioribosylzeatin in the tRNA of Salmonella Cell 36, 523-531
    • (1984) Cell , vol.36 , pp. 523-531
    • Buck, M.1    Ames, B.N.2
  • 19
    • 0028986353 scopus 로고
    • 6A) present next to the anticodon contributes to the decoding efficiency of the tRNA
    • 6A) present next to the anticodon contributes to the decoding efficiency of the tRNA J. Bacteriol. 177, 1967-1975
    • (1995) J. Bacteriol. , vol.177 , pp. 1967-1975
    • Esberg, B.1    Björk, G.R.2
  • 20
    • 0021806595 scopus 로고
    • Presence of 2-methylthioribosyl-trans-zeatin in Azotobacter vinelandii tRNA
    • Ajitkumar, P. and Cherayil, J. D. (1985) Presence of 2-methylthioribosyl-trans-zeatin in Azotobacter vinelandii tRNA J. Bacteriol. 162, 752-755
    • (1985) J. Bacteriol. , vol.162 , pp. 752-755
    • Ajitkumar, P.1    Cherayil, J.D.2
  • 24
    • 0009411657 scopus 로고
    • Reactions of non-heme iron(II) centers with dioxygen in biology and chemistry
    • Feig, A. L. and Lippard, S. (1994) Reactions of non-heme iron(II) centers with dioxygen in biology and chemistry Chem. Rev. 94, 759-805
    • (1994) Chem. Rev. , vol.94 , pp. 759-805
    • Feig, A.L.1    Lippard, S.2
  • 25
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron clusters
    • Wallar, B. J. and Lipscomb, J. D. (1996) Dioxygen activation by enzymes containing binuclear non-heme iron clusters Chem. Rev. 96, 2625-2658
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2658
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 28
    • 0037381328 scopus 로고    scopus 로고
    • Evolution of Bacterial and Archaeal multicomponent monooxygenases
    • Notomista, E., Lahm, A., Di Donato, A., and Tramontano, A. (2003) Evolution of Bacterial and Archaeal multicomponent monooxygenases J. Mol. Evol. 56, 435-445
    • (2003) J. Mol. Evol. , vol.56 , pp. 435-445
    • Notomista, E.1    Lahm, A.2    Di Donato, A.3    Tramontano, A.4
  • 29
    • 0032552881 scopus 로고    scopus 로고
    • 9-desaturase: Oxidase reactivity during single turnover and implications for the mechanism of desaturation
    • 9-desaturase: Oxidase reactivity during single turnover and implications for the mechanism of desaturation Biochemistry 37, 14664-14671
    • (1998) Biochemistry , vol.37 , pp. 14664-14671
    • Broadwater, J.A.1    Ai, J.2    Loehr, T.M.3    Sanders-Loehr, J.4    Fox, B.G.5
  • 30
    • 0023655427 scopus 로고
    • Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli
    • Sjöberg, B. M., Karlsson, M., and Jornvall, H. (1987) Half-site reactivity of the tyrosyl radical of ribonucleotide reductase from Escherichia coli J. Biol. Chem. 262, 9736-9743
    • (1987) J. Biol. Chem. , vol.262 , pp. 9736-9743
    • Sjöberg, B.M.1    Karlsson, M.2    Jornvall, H.3
  • 31
    • 0035964255 scopus 로고    scopus 로고
    • Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4
    • Ge, J., Perlstein, D. L., Nguyen, H. H., Bar, G., Griffin, R. G., and Stubbe, J. (2001) Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4 Proc. Natl. Acad. Sci. U.S.A. 98, 10067-10072
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10067-10072
    • Ge, J.1    Perlstein, D.L.2    Nguyen, H.H.3    Bar, G.4    Griffin, R.G.5    Stubbe, J.6
  • 33
    • 0037846477 scopus 로고    scopus 로고
    • Rapid-Mix and Chemical Quench Studies of Ferredoxin-Reduced Stearoyl-Acyl Carrier Protein Desaturase
    • Lyle, K. S., Haas, J. A., and Fox, B. G. (2003) Rapid-Mix and Chemical Quench Studies of Ferredoxin-Reduced Stearoyl-Acyl Carrier Protein Desaturase Biochemistry 42, 5857-5866
    • (2003) Biochemistry , vol.42 , pp. 5857-5866
    • Lyle, K.S.1    Haas, J.A.2    Fox, B.G.3
  • 34
    • 0037560872 scopus 로고    scopus 로고
    • Mechanistic studies on the hydroxylation of methane by methane monooxygenase
    • Baik, M. H., Newcomb, M., Friesner, R. A., and Lippard, S. J. (2003) Mechanistic studies on the hydroxylation of methane by methane monooxygenase Chem. Rev. 103, 2385-2419
    • (2003) Chem. Rev. , vol.103 , pp. 2385-2419
    • Baik, M.H.1    Newcomb, M.2    Friesner, R.A.3    Lippard, S.J.4
  • 35
    • 70349776273 scopus 로고    scopus 로고
    • Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase
    • Bailey, L. J. and Fox, B. G. (2009) Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase Biochemistry 48, 8932-8939
    • (2009) Biochemistry , vol.48 , pp. 8932-8939
    • Bailey, L.J.1    Fox, B.G.2
  • 36
    • 0026630133 scopus 로고
    • Methane Monooxygenase Component B and Reductase Alter the Regioselectivity of the Hydroxylase Component-catalyzed Reactions
    • Froland, W. A., Andersson, K. K., Lee, S.-K., Liu, Y., and Lipscomb, J. D. (1992) Methane Monooxygenase Component B and Reductase Alter the Regioselectivity of the Hydroxylase Component-catalyzed Reactions J. Biol. Chem. 267, 17588-17597
    • (1992) J. Biol. Chem. , vol.267 , pp. 17588-17597
    • Froland, W.A.1    Andersson, K.K.2    Lee, S.-K.3    Liu, Y.4    Lipscomb, J.D.5
  • 37
    • 34547768909 scopus 로고    scopus 로고
    • Substrate trafficking and dioxygen activation in bacterial multicomponent monooxygenases
    • Murray, L. J. and Lippard, S. J. (2007) Substrate trafficking and dioxygen activation in bacterial multicomponent monooxygenases Acc. Chem. Res. 40, 466-474
    • (2007) Acc. Chem. Res. , vol.40 , pp. 466-474
    • Murray, L.J.1    Lippard, S.J.2
  • 38
    • 33748433282 scopus 로고    scopus 로고
    • Correlating Structure with Function in Bacterial Multicomponent Monooxygenases and Related Diiron Proteins
    • Sazinsky, M. H. and Lippard, S. J. (2006) Correlating Structure with Function in Bacterial Multicomponent Monooxygenases and Related Diiron Proteins Acc. Chem. Res. 39, 558-566
    • (2006) Acc. Chem. Res. , vol.39 , pp. 558-566
    • Sazinsky, M.H.1    Lippard, S.J.2
  • 39
    • 0037022829 scopus 로고    scopus 로고
    • Combined Participation of Hydroxylase Active Site Residues and Effector Protein Binding in a Para to Ortho Modulation of Toluene 4-Monooxygenase Regiospecificity
    • Mitchell, K. H., Studts, J. M., and Fox, B. G. (2002) Combined Participation of Hydroxylase Active Site Residues and Effector Protein Binding in a Para to Ortho Modulation of Toluene 4-Monooxygenase Regiospecificity Biochemistry 41, 3176-3188
    • (2002) Biochemistry , vol.41 , pp. 3176-3188
    • Mitchell, K.H.1    Studts, J.M.2    Fox, B.G.3
  • 40
    • 0028889024 scopus 로고
    • Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S]ferredoxin
    • Cheng, H., Westler, W. M., Xia, B., Oh, B. H., and Markley, J. L. (1995) Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S]ferredoxin Arch. Biochem. Biophys. 316, 619-634
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 619-634
    • Cheng, H.1    Westler, W.M.2    Xia, B.3    Oh, B.H.4    Markley, J.L.5
  • 41
    • 0029379752 scopus 로고
    • Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21 (DE3): Process control yielding high levels of metal-incorporated, soluble protein
    • Hoffman, B. J., Broadwater, J. A., Johnson, P., Harper, J., Fox, B. G., and Kenealy, W. R. (1995) Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21 (DE3): Process control yielding high levels of metal-incorporated, soluble protein Protein Expression Purif. 6, 646-654
    • (1995) Protein Expression Purif. , vol.6 , pp. 646-654
    • Hoffman, B.J.1    Broadwater, J.A.2    Johnson, P.3    Harper, J.4    Fox, B.G.5    Kenealy, W.R.6
  • 42
    • 0030926773 scopus 로고    scopus 로고
    • Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12
    • Leung, H. C., Chen, Y., and Winkler, M. E. (1997) Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12 J. Biol. Chem. 272, 13073-13083
    • (1997) J. Biol. Chem. , vol.272 , pp. 13073-13083
    • Leung, H.C.1    Chen, Y.2    Winkler, M.E.3
  • 43
    • 0024362769 scopus 로고
    • Ribonucleoside Analysis by Reversed-Phase High-Performance Liquid-Chromatography
    • Gehrke, C. W. and Kuo, K. C. (1989) Ribonucleoside Analysis by Reversed-Phase High-Performance Liquid-Chromatography J. Chromatogr. 471, 3-36
    • (1989) J. Chromatogr. , vol.471 , pp. 3-36
    • Gehrke, C.W.1    Kuo, K.C.2
  • 44
    • 84986850849 scopus 로고
    • Tandem mass spectrometry (MS/MS) instrumentation
    • Yost, R. A. and Fetterolf, D. D. (1983) Tandem mass spectrometry (MS/MS) instrumentation Mass Spectrom. Rev. 2, 1-45
    • (1983) Mass Spectrom. Rev. , vol.2 , pp. 1-45
    • Yost, R.A.1    Fetterolf, D.D.2
  • 45
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N. J. (2007) Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 1, 2876-2890
    • (2007) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 48
    • 0034827514 scopus 로고    scopus 로고
    • Correlations of structure and electronic properties from EPR spectroscopy of hydroxylamine oxidoreductase
    • Hendrich, M. P., Petasis, D., Arciero, D. M., and Hooper, A. B. (2001) Correlations of structure and electronic properties from EPR spectroscopy of hydroxylamine oxidoreductase J. Am. Chem. Soc. 123, 2997-3005
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2997-3005
    • Hendrich, M.P.1    Petasis, D.2    Arciero, D.M.3    Hooper, A.B.4
  • 50
    • 84900533037 scopus 로고    scopus 로고
    • Mössbauer, EPR, and Modeling Study of Iron Trafficking and Regulation in Δccc1 and CCC1-up Saccharomyces cerevisiae
    • Cockrell, A., McCormick, S. P., Moore, M. J., Chakrabarti, M., and Lindahl, P. A. (2014) Mössbauer, EPR, and Modeling Study of Iron Trafficking and Regulation in Δccc1 and CCC1-up Saccharomyces cerevisiae Biochemistry 53, 2926-2940
    • (2014) Biochemistry , vol.53 , pp. 2926-2940
    • Cockrell, A.1    McCormick, S.P.2    Moore, M.J.3    Chakrabarti, M.4    Lindahl, P.A.5
  • 51
    • 0014958368 scopus 로고
    • Mass spectrometry of nucleic acid components. Analogs of adenosine
    • Shaw, S. J., Desiderio, D. M., Tsuboyama, K., and McCloskey, J. A. (1970) Mass spectrometry of nucleic acid components. Analogs of adenosine J. Am. Chem. Soc. 92, 2510-2522
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 2510-2522
    • Shaw, S.J.1    Desiderio, D.M.2    Tsuboyama, K.3    McCloskey, J.A.4
  • 53
    • 0037846477 scopus 로고    scopus 로고
    • Rapid-mix and chemical quench studies of ferredoxin-reduced stearoyl-acyl carrier protein desaturase
    • Lyle, K. S., Haas, J. A., and Fox, B. G. (2003) Rapid-mix and chemical quench studies of ferredoxin-reduced stearoyl-acyl carrier protein desaturase Biochemistry 42, 5857-5866
    • (2003) Biochemistry , vol.42 , pp. 5857-5866
    • Lyle, K.S.1    Haas, J.A.2    Fox, B.G.3
  • 54
    • 0029942829 scopus 로고    scopus 로고
    • Recombinant toluene-4-monooxygenase: Catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex
    • Pikus, J. D., Studts, J. M., Achim, C., Kauffmann, K. E., Münck, E., Steffan, R. J., McClay, K., and Fox, B. G. (1996) Recombinant toluene-4-monooxygenase: Catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex Biochemistry 35, 9106-9119
    • (1996) Biochemistry , vol.35 , pp. 9106-9119
    • Pikus, J.D.1    Studts, J.M.2    Achim, C.3    Kauffmann, K.E.4    Münck, E.5    Steffan, R.J.6    McClay, K.7    Fox, B.G.8
  • 55
    • 0037183499 scopus 로고    scopus 로고
    • Biochemical, Mössbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. Strain CF 600
    • Cadieux, E., Vrajmasu, V., Achim, C., Powlowski, J., and Münck, E. (2002) Biochemical, Mössbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600 Biochemistry 41, 10680-10691
    • (2002) Biochemistry , vol.41 , pp. 10680-10691
    • Cadieux, E.1    Vrajmasu, V.2    Achim, C.3    Powlowski, J.4    Münck, E.5
  • 56
    • 0024728608 scopus 로고
    • Integer-spin electron paramagnetic resonance of iron proteins
    • Hendrich, M. P. and Debrunner, P. G. (1989) Integer-spin electron paramagnetic resonance of iron proteins Biophys. J. 56, 489-506
    • (1989) Biophys. J. , vol.56 , pp. 489-506
    • Hendrich, M.P.1    Debrunner, P.G.2
  • 57
    • 0032500321 scopus 로고    scopus 로고
    • Modeling the Diiron Centers of Non-Heme Iron Enzymes. Preparation of Sterically Hindered Diiron(II) Tetracarboxylate Complexes and Their Reactions with Dioxygen
    • LeCloux, D. D., Barrios, A. M., Mizoguchi, T. J., and Lippard, S. J. (1998) Modeling the Diiron Centers of Non-Heme Iron Enzymes. Preparation of Sterically Hindered Diiron(II) Tetracarboxylate Complexes and Their Reactions with Dioxygen J. Am. Chem. Soc. 120, 9001-9014
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9001-9014
    • Lecloux, D.D.1    Barrios, A.M.2    Mizoguchi, T.J.3    Lippard, S.J.4
  • 59
    • 0019872615 scopus 로고
    • Mössbauer spectroscopic studies of hemerythrin from Phascolosoma lurco (syn. Phascolosoma Arcuatum)
    • Clark, P. E. and Webb, J. (1981) Mössbauer spectroscopic studies of hemerythrin from Phascolosoma lurco (syn. Phascolosoma Arcuatum) Biochemistry 20, 4628-4632
    • (1981) Biochemistry , vol.20 , pp. 4628-4632
    • Clark, P.E.1    Webb, J.2
  • 60
    • 0024474698 scopus 로고
    • Mössbauer and EPR studies of the binuclear iron center in ribonucleotide reductase from Escherichia coli. A new iron-to-protein stoichiometry
    • Lynch, J. B., Juarez-Garcia, C., Münck, E., and Que, L. (1989) Mössbauer and EPR studies of the binuclear iron center in ribonucleotide reductase from Escherichia coli. A new iron-to-protein stoichiometry J. Biol. Chem. 264, 8091-8096
    • (1989) J. Biol. Chem. , vol.264 , pp. 8091-8096
    • Lynch, J.B.1    Juarez-Garcia, C.2    Münck, E.3    Que, L.4
  • 62
    • 0001016575 scopus 로고
    • Mössbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox, B. G., Hendrich, M. P., Surerus, K. K., Andersson, K. K., Froland, W. A., Lipscomb, J. D., and Münck, E. (1993) Mössbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b J. Am. Chem. Soc. 115, 3688-3701
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3688-3701
    • Fox, B.G.1    Hendrich, M.P.2    Surerus, K.K.3    Andersson, K.K.4    Froland, W.A.5    Lipscomb, J.D.6    Münck, E.7
  • 63
    • 84922441520 scopus 로고    scopus 로고
    • The Limits for Life Define the Limits for Enzymes
    • Chapter 2, Springer, New York
    • Traut, T. (2008) The Limits for Life Define the Limits for Enzymes. Allosteric Regulatory Enzymes, Chapter 2, Springer, New York.
    • (2008) Allosteric Regulatory Enzymes
    • Traut, T.1


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