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Volumn 50, Issue 33, 2011, Pages 7132-7145

Dominant intermediate charcot-marie-tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYLATION; GLUTAMIC ACID; ONE-FORM; PERIPHERAL NEUROPATHY; RECOMBINANT PROTEIN; SYNTHETASES;

EID: 80051754461     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200989h     Document Type: Article
Times cited : (41)

References (59)
  • 1
    • 80051710290 scopus 로고    scopus 로고
    • National Institute of Neurological Disorders and Stroke (NINDS), Washington, D.C.
    • Charcot-Marie-Tooth Disease Fact Sheet (2003), National Institute of Neurological Disorders and Stroke (NINDS), Washington, D.C.
    • (2003) Charcot-Marie-Tooth Disease Fact Sheet
  • 2
    • 8544257332 scopus 로고    scopus 로고
    • Charcot-marie-tooth disease (hereditary motor sensory neuropathies) and hereditary sensory and autonomic neuropathies
    • DOI 10.1097/01.nrl.0000145596.38640.27
    • Bertorini, T., Narayanaswami, P., and Rashed, H. (2004) Charcot-Marie-Tooth disease (hereditary motor sensory neuropathies) and hereditary sensory and autonomic neuropathies Neurologist 10, 327-337 (Pubitemid 39492078)
    • (2004) Neurologist , vol.10 , Issue.6 , pp. 327-337
    • Bertorini, T.1    Narayanaswami, P.2    Rashed, H.3
  • 3
    • 33644523786 scopus 로고    scopus 로고
    • Peripheral neuropathies caused by mutations in the myelin protein zero
    • Shy, M. E. (2006) Peripheral neuropathies caused by mutations in the myelin protein zero J. Neurol. Sci. 242, 55-66
    • (2006) J. Neurol. Sci. , vol.242 , pp. 55-66
    • Shy, M.E.1
  • 9
    • 0037177828 scopus 로고    scopus 로고
    • Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase
    • DOI 10.1074/jbc.M103396200
    • Austin, J. and First, E. A. (2002) Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase J. Biol. Chem. 277, 14812-14820 (Pubitemid 34952553)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14812-14820
    • Austin, J.1    First, E.A.2
  • 10
    • 0027232291 scopus 로고
    • Reaction of modified and unmodified tRNA(Tyr) substrates with tyrosyl- tRNA synthetase (Bacillus stearothermophilus)
    • Avis, J. M., Day, A. G., Garcia, G. A., and Fersht, A. R. (1993) Reaction of modified and unmodified tRNA(Tyr) substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus) Biochemistry 32, 5312-5320 (Pubitemid 23167971)
    • (1993) Biochemistry , vol.32 , Issue.20 , pp. 5312-5320
    • Avis, J.M.1    Day, A.G.2    Garcia, G.A.3    Fersht, A.R.4
  • 11
    • 0016437582 scopus 로고
    • Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase
    • Fersht, A. R., Mulvey, R. S., and Koch, G. L. (1975) Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase Biochemistry 14, 13-18
    • (1975) Biochemistry , vol.14 , pp. 13-18
    • Fersht, A.R.1    Mulvey, R.S.2    Koch, G.L.3
  • 12
    • 0016432066 scopus 로고
    • Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes
    • Fersht, A. R. (1975) Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes Biochemistry 14, 5-12
    • (1975) Biochemistry , vol.14 , pp. 5-12
    • Fersht, A.R.1
  • 13
    • 0030945598 scopus 로고    scopus 로고
    • Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine
    • DOI 10.1074/jbc.272.22.14420
    • Kleeman, T. A., Wei, D., Simpson, K. L., and First, E. A. (1997) Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine J. Biol. Chem. 272, 14420-14425 (Pubitemid 27232860)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14420-14425
    • Kleeman, T.A.1    Wei, D.2    Simpson, K.L.3    First, E.A.4
  • 14
    • 0037036396 scopus 로고    scopus 로고
    • Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase
    • DOI 10.1074/jbc.M201923200
    • Austin, J. and First, E. A. (2002) Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase J. Biol. Chem. 277, 20243-20248 (Pubitemid 34967316)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20243-20248
    • Austin, J.1    First, E.A.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0034681169 scopus 로고    scopus 로고
    • The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr)
    • DOI 10.1021/bi991675l
    • Xin, Y., Li, W., and First, E. A. (2000) The 'KMSKS' motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr) Biochemistry 39, 340-347 (Pubitemid 30056468)
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 340-347
    • Xin, Y.1    Li, W.2    First, E.A.3
  • 20
    • 38749146474 scopus 로고    scopus 로고
    • Predicting ultraviolet spectrum of single stranded and double stranded deoxyribonucleic acids
    • Tataurov, A. V., You, Y., and Owczarzy, R. (2008) Predicting ultraviolet spectrum of single stranded and double stranded deoxyribonucleic acids Biophys. Chem. 133, 66-70
    • (2008) Biophys. Chem. , vol.133 , pp. 66-70
    • Tataurov, A.V.1    You, Y.2    Owczarzy, R.3
  • 21
    • 0016699947 scopus 로고
    • Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation
    • Jakes, R. and Fersht, A. R. (1975) Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation Biochemistry 14, 3344-3350
    • (1975) Biochemistry , vol.14 , pp. 3344-3350
    • Jakes, R.1    Fersht, A.R.2
  • 22
    • 48849103642 scopus 로고    scopus 로고
    • Quantitative determination of protein stability and ligand binding by pulse proteolysis
    • Chapter 20, Unit 20 11.
    • Park, C. and Marqusee, S. (2006) Quantitative determination of protein stability and ligand binding by pulse proteolysis. Curr. Protoc. Protein Sci., Chapter 20, Unit 20 11.
    • (2006) Curr. Protoc. Protein Sci.
    • Park, C.1    Marqusee, S.2
  • 23
    • 0016437581 scopus 로고
    • Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases
    • Fersht, A. R., Ashford, J. S., Bruton, C. J., Jakes, R., Koch, G. L., and Hartley, B. S. (1975) Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases Biochemistry 14, 1-4
    • (1975) Biochemistry , vol.14 , pp. 1-4
    • Fersht, A.R.1    Ashford, J.S.2    Bruton, C.J.3    Jakes, R.4    Koch, G.L.5    Hartley, B.S.6
  • 24
    • 45149108596 scopus 로고    scopus 로고
    • Activation of D-tyrosine by Bacillus stearothermophilus tyrosyl-tRNA synthetase: 1. Pre-steady-state kinetic analysis reveals the mechanistic basis for the recognition of D-tyrosine
    • Sheoran, A., Sharma, G., and First, E. A. (2008) Activation of D-tyrosine by Bacillus stearothermophilus tyrosyl-tRNA synthetase: 1. Pre-steady-state kinetic analysis reveals the mechanistic basis for the recognition of D-tyrosine J. Biol. Chem. 283, 12960-12970
    • (2008) J. Biol. Chem. , vol.283 , pp. 12960-12970
    • Sheoran, A.1    Sharma, G.2    First, E.A.3
  • 25
    • 80051771712 scopus 로고
    • Analysis of Ligand Binding by Enzymes
    • (Engel, P. Ed.) 1 st ed. Chapter 6, pp, Academic Press, New York.
    • Clarke, A. R. (1966) Analysis of Ligand Binding by Enzymes, in Enzymology Labfax (Engel, P., Ed.) 1 st ed., Chapter 6, pp 201-205, Academic Press, New York.
    • (1966) Enzymology Labfax , pp. 201-205
    • Clarke, A.R.1
  • 26
    • 4043158815 scopus 로고
    • The constitution and fundamental properties of solids and liquids, i - Solids
    • Langmuir, I. (1916) The constitution and fundamental properties of solids and liquids, I-Solids J. Am. Chem. Soc. 38, 2221-2295
    • (1916) J. Am. Chem. Soc. , vol.38 , pp. 2221-2295
    • Langmuir, I.1
  • 27
    • 84969001783 scopus 로고
    • The attactions of proteins for small molecules and ions
    • Scatchard, G. (1948) The attactions of proteins for small molecules and ions Ann. N.Y. Acad. Sci. 51, 660-672
    • (1948) Ann. N.Y. Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 28
    • 0000870544 scopus 로고
    • Die Kinetik der Invertinwirkung
    • Michaelis, L. and Menten, M. (1913) Die Kinetik der Invertinwirkung Biochem. Z. 49, 333-369
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.2
  • 29
    • 0003818741 scopus 로고    scopus 로고
    • 1 st ed. pp, Academic Press, San Diego.
    • Engel, P. (1996) Enzymology Labfax, 1 st ed., pp 200-210, Academic Press, San Diego.
    • (1996) Enzymology Labfax , pp. 200-210
    • Engel, P.1
  • 30
    • 3242801426 scopus 로고
    • A Comparison of Estimates of Michaelis-Menten Kinetic Constants from Various Linear Transformations
    • Dowd, J. E. and Riggs, D. S. (1965) A Comparison of Estimates of Michaelis-Menten Kinetic Constants from Various Linear Transformations J. Biol. Chem. 240, 863-869
    • (1965) J. Biol. Chem. , vol.240 , pp. 863-869
    • Dowd, J.E.1    Riggs, D.S.2
  • 31
    • 0002372921 scopus 로고
    • The inhibition of cholinesterase by physostigmine and prostigmine
    • Eadie, G. S. (1942) The inhibition of cholinesterase by physostigmine and prostigmine J. Biol. Chem. 146, 85-93
    • (1942) J. Biol. Chem. , vol.146 , pp. 85-93
    • Eadie, G.S.1
  • 32
    • 0001395234 scopus 로고
    • Non-inverted versus inverted plots in enzyme kinetics
    • Hofstee, B. H. (1959) Non-inverted versus inverted plots in enzyme kinetics Nature 184, 1296-1298
    • (1959) Nature , vol.184 , pp. 1296-1298
    • Hofstee, B.H.1
  • 33
    • 0022471120 scopus 로고
    • Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase
    • Wells, T. N. and Fersht, A. R. (1986) Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase Biochemistry 25, 1881-1886 (Pubitemid 16035996)
    • (1986) Biochemistry , vol.25 , Issue.8 , pp. 1881-1886
    • Wells, T.N.C.1    Fersht, A.R.2
  • 35
    • 0042785196 scopus 로고    scopus 로고
    • Expression, purification, and characterization of human tyrosyl-tRNA synthetase
    • DOI 10.1016/S1046-5928(02)00576-4, PII S1046592802005764
    • Jia, J., Li, B., Jin, Y., and Wang, D. (2003) Expression, purification, and characterization of human tyrosyl-tRNA synthetase Protein Expression Purif. 27, 104-108 (Pubitemid 37096476)
    • (2003) Protein Expression and Purification , vol.27 , Issue.1 , pp. 104-108
    • Jia, J.1    Li, B.2    Jin, Y.3    Wang, D.4
  • 36
    • 0021795227 scopus 로고
    • Charcot-Marie-Tooth disease: Study of a large kinship with an intermediate form
    • DOI 10.1007/BF00313907
    • Rossi, A., Paradiso, C., Cioni, R., Rizzuto, N., and Guazzi, G. (1985) Charcot-Marie-Tooth disease: study of a large kinship with an intermediate form J. Neurol. 232, 91-98 (Pubitemid 15059920)
    • (1985) Journal of Neurology , vol.232 , Issue.2 , pp. 91-98
    • Rossi, A.1    Paradiso, C.2    Cioni, R.3
  • 39
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • DOI 10.1126/science.284.5411.147
    • Wakasugi, K. and Schimmel, P. (1999) Two distinct cytokines released from a human aminoacyl-tRNA synthetase Science (New York, N.Y.) 284, 147-151 (Pubitemid 29282068)
    • (1999) Science , vol.284 , Issue.5411 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 40
    • 71549128376 scopus 로고    scopus 로고
    • Functional expansion of human tRNA synthetases achieved by structural inventions
    • Guo, M., Schimmel, P., and Yang, X. L. (2010) Functional expansion of human tRNA synthetases achieved by structural inventions FEBS Lett. 584, 434-442
    • (2010) FEBS Lett. , vol.584 , pp. 434-442
    • Guo, M.1    Schimmel, P.2    Yang, X.L.3
  • 41
    • 57649138442 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase is a target for mutant SOD1 toxicity in mitochondria
    • Kawamata, H., Magrane, J., Kunst, C., King, M. P., and Manfredi, G. (2008) Lysyl-tRNA synthetase is a target for mutant SOD1 toxicity in mitochondria J. Biol. Chem. 283, 28321-28328
    • (2008) J. Biol. Chem. , vol.283 , pp. 28321-28328
    • Kawamata, H.1    Magrane, J.2    Kunst, C.3    King, M.P.4    Manfredi, G.5
  • 43
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • Aguzzi, A. and O'Connor, T. Protein aggregation diseases: pathogenicity and therapeutic perspectives, Nat. Rev. Drug Discovery 9, 237-248.
    • Nat. Rev. Drug Discovery , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 45
    • 0034701008 scopus 로고    scopus 로고
    • Identity of tRNA for yeast tyrosyl-tRNA synthetase: Tyrosylation is more sensitive to identity nucleotides than to structural features
    • DOI 10.1021/bi992276t
    • Fechter, P., Rudinger-Thirion, J., Theobald-Dietrich, A., and Giege, R. (2000) Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features Biochemistry 39, 1725-1733 (Pubitemid 30108963)
    • (2000) Biochemistry , vol.39 , Issue.7 , pp. 1725-1733
    • Fechter, P.1    Rudinger-Thirion, J.2    Theobald-Dietrich, A.3    Giege, R.4
  • 46
    • 33746189733 scopus 로고    scopus 로고
    • Distinct Kinetic Mechanisms of the Two Classes of Aminoacyl-tRNA Synthetases
    • DOI 10.1016/j.jmb.2006.06.015, PII S002228360600725X
    • Zhang, C. M., Perona, J. J., Ryu, K., Francklyn, C., and Hou, Y. M. (2006) Distinct kinetic mechanisms of the two classes of Aminoacyl-tRNA synthetases J. Mol. Biol. 361, 300-311 (Pubitemid 44092779)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.2 , pp. 300-311
    • Zhang, C.-M.1    Perona, J.J.2    Ryu, K.3    Francklyn, C.4    Hou, Y.-M.5
  • 47
    • 35348920149 scopus 로고    scopus 로고
    • Hydrolysis of non-cognate aminoacyl-adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain
    • DOI 10.1016/j.febslet.2007.09.058, PII S0014579307010423
    • Gruic-Sovulj, I., Rokov-Plavec, J., and Weygand-Durasevic, I. (2007) Hydrolysis of non-cognate aminoacyl-adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain FEBS Lett. 581, 5110-5114 (Pubitemid 47576095)
    • (2007) FEBS Letters , vol.581 , Issue.26 , pp. 5110-5114
    • Gruic-Sovulj, I.1    Rokov-Plavec, J.2    Weygand-Durasevic, I.3
  • 52
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N.
    • Collaborative Computational Project, N. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 53
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. 60, 2256-2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 54
    • 0023868490 scopus 로고
    • Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: A mobile loop envelopes the transition state in an induced-fit mechanism
    • Fersht, A. R., Knill-Jones, J. W., Bedouelle, H., and Winter, G. (1988) Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism Biochemistry 27, 1581-1587 (Pubitemid 18077451)
    • (1988) Biochemistry , vol.27 , Issue.5 , pp. 1581-1587
    • Fersht, A.R.1    Knill-Jones, J.W.2    Bedouelle, H.3    Winter, G.4
  • 55
    • 0023674455 scopus 로고
    • Tyrosyl-tRNA synthetase from the bovine liver. Isolation and physico-chemical properties
    • Korneliuk, A. I., Kurochkin, I. V., and Matsuka, G. (1988) [Tyrosyl-tRNA synthetase from the bovine liver. Isolation and physico-chemical properties] Mol. Biol. (Kiev) 22, 176-186
    • (1988) Mol. Biol. (Kiev) , vol.22 , pp. 176-186
    • Korneliuk, A.I.1    Kurochkin, I.V.2    Matsuka, G.3
  • 56
    • 0018124327 scopus 로고
    • Purification and some properties of rat liver tyrosyl-tRNA synthetase
    • Deak, F. and Denes, G. (1978) Purification and some properties of rat liver tyrosyl-tRNA synthetase Biochim. Biophys. Acta 526, 626-634 (Pubitemid 9043282)
    • (1978) Biochimica et Biophysica Acta , vol.526 , Issue.2 , pp. 626-634
    • Deak, F.1    Denes, G.2
  • 57
    • 0017117764 scopus 로고
    • Mechanisms of suppression in Drosophila. IV. Specificity and properties of tyrosyl-tRNA synthetase
    • Warner, C. K. and Jacobson, K. B. (1976) Mechanisms of suppression in Drosophila. IV. Specificity and properties of tyrosyl-tRNA synthetase Can. J. Biochem. 54, 650-656
    • (1976) Can. J. Biochem. , vol.54 , pp. 650-656
    • Warner, C.K.1    Jacobson, K.B.2
  • 58
    • 0015860034 scopus 로고
    • Purification of tyrosine: TRNA ligase from Saccharomyces cerevisiae alphaS288C
    • Kucan, Z. and Chambers, R. W. (1973) Purification of tyrosine: tRNA ligase from Saccharomyces cerevisiae alphaS288C J. Biochem. 73, 811-819
    • (1973) J. Biochem. , vol.73 , pp. 811-819
    • Kucan, Z.1    Chambers, R.W.2
  • 59
    • 0024297210 scopus 로고
    • Tyrosyl-tRNA synthetase from wheat germ
    • Quivy, J. P. and Chroboczek, J. (1988) Tyrosyl-tRNA synthetase from wheat germ J. Biol. Chem. 263, 15277-15281
    • (1988) J. Biol. Chem. , vol.263 , pp. 15277-15281
    • Quivy, J.P.1    Chroboczek, J.2


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