메뉴 건너뛰기




Volumn 46, Issue 17, 2007, Pages 5170-5176

A unique insert of leucyl-tRNA synthetase is required for aminoacylation and not amino acid editing

Author keywords

[No Author keywords available]

Indexed keywords

ACYLATION; AMINO ACIDS; ESCHERICHIA COLI; NUCLEOTIDES; RNA; SUBSTRATES;

EID: 34247581696     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062078j     Document Type: Article
Times cited : (9)

References (39)
  • 1
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M., and Söll, D. (2000) Aminoacyl-tRNA synthesis, Annu. Rev. Biochem. 69, 617-650.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 2
    • 0033198765 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: A family of expanding functions
    • Martinis, S. A., Plateau, P., Cavarelli, J., and Florentz, C. (1999) Aminoacyl-tRNA synthetases: a family of expanding functions, EMBO J. 18, 4591-4596.
    • (1999) EMBO J , vol.18 , pp. 4591-4596
    • Martinis, S.A.1    Plateau, P.2    Cavarelli, J.3    Florentz, C.4
  • 3
    • 33747362545 scopus 로고    scopus 로고
    • Leucyl-tRNA synthetase
    • Ibba, M, Francklyn, C, and Cusack, S, Eds, pp, Landes Bioscience, Georgetown, TX
    • Lincecum, T. L., Jr., and Martinis, S. A. (2005) Leucyl-tRNA synthetase, in The Aminoacyl-tRNA Synthetases (Ibba, M., Francklyn, C., and Cusack, S., Eds.) pp 36-47, Landes Bioscience, Georgetown, TX.
    • (2005) The Aminoacyl-tRNA Synthetases , pp. 36-47
    • Lincecum Jr., T.L.1    Martinis, S.A.2
  • 4
    • 1542563485 scopus 로고
    • Evolutionary and structural relationships among dehydrogenases
    • Boyer, P. D, Ed, 3rd ed, pp, Academic Press, New York
    • Rossmann, M. G., Liljas, A., Branden, C. I., and Banaszak, L. J. (1975) Evolutionary and structural relationships among dehydrogenases, in The Enzymes (Boyer, P. D., Ed.) 3rd ed., pp 61-102, Academic Press, New York.
    • (1975) The Enzymes , pp. 61-102
    • Rossmann, M.G.1    Liljas, A.2    Branden, C.I.3    Banaszak, L.J.4
  • 5
    • 0034657687 scopus 로고    scopus 로고
    • The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue
    • Cusack, S., Yaremchuk, A., and Tukalo, M. (2000) The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue, EMBO J. 19, 2351-2361.
    • (2000) EMBO J , vol.19 , pp. 2351-2361
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 6
    • 0026087217 scopus 로고
    • Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase
    • Hou, Y. M., Shiba, K., Mottes, C., and Schimmel, P. (1991) Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase, Proc. Natl. Acad. Sci. U.S.A. 88, 976-980.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 976-980
    • Hou, Y.M.1    Shiba, K.2    Mottes, C.3    Schimmel, P.4
  • 7
    • 0026075798 scopus 로고
    • Structural relationships and the classification of aminoacyl-tRNA synthetases
    • Burbaum, J. J., and Schimmel, P. (1991) Structural relationships and the classification of aminoacyl-tRNA synthetases, J. Biol. Chem. 266, 16965-16968.
    • (1991) J. Biol. Chem , vol.266 , pp. 16965-16968
    • Burbaum, J.J.1    Schimmel, P.2
  • 8
    • 0023202876 scopus 로고
    • Evidence for dispensable sequences inserted into a nucleotide fold
    • Starzyk, R. M., Webster, T. A., and Schimmel, P. (1987) Evidence for dispensable sequences inserted into a nucleotide fold, Science 237, 1614-1618.
    • (1987) Science , vol.237 , pp. 1614-1618
    • Starzyk, R.M.1    Webster, T.A.2    Schimmel, P.3
  • 10
    • 12344309250 scopus 로고    scopus 로고
    • Crystal structure of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii reveals a novel editing domain orientation
    • Fukunaga, R., and Yokoyama, S. (2005) Crystal structure of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii reveals a novel editing domain orientation, J. Mol. Biol. 346, 57-71.
    • (2005) J. Mol. Biol , vol.346 , pp. 57-71
    • Fukunaga, R.1    Yokoyama, S.2
  • 11
    • 2942670336 scopus 로고    scopus 로고
    • Two distinct domains of the β subunit of Aquifex Aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection
    • Zheng, Y. G., Wei, H., Ling, C., Martin, F., Eriani, G., and Wang, E. D. (2004) Two distinct domains of the β subunit of Aquifex Aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection, Nucleic Acids Res. 32, 3294-3303.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3294-3303
    • Zheng, Y.G.1    Wei, H.2    Ling, C.3    Martin, F.4    Eriani, G.5    Wang, E.D.6
  • 12
    • 33747338033 scopus 로고    scopus 로고
    • Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles
    • Hsu, J. L., Rho, S. B., Vanella, K. M., and Martinis, S. A. (2006) Functional divergence of a unique C-terminal domain of leucyl-tRNA synthetase to accommodate its splicing and aminoacylation roles, J. Biol. Chem. 281, 23075-23082.
    • (2006) J. Biol. Chem , vol.281 , pp. 23075-23082
    • Hsu, J.L.1    Rho, S.B.2    Vanella, K.M.3    Martinis, S.A.4
  • 13
    • 27144523803 scopus 로고    scopus 로고
    • leu from the archaeon Pyrococcus horikoshii, Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 61, 30-32.
    • leu from the archaeon Pyrococcus horikoshii, Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 61, 30-32.
  • 14
    • 27144520077 scopus 로고    scopus 로고
    • leu reveal two modes of discriminator-base recognition
    • leu reveal two modes of discriminator-base recognition, Nat. Struct. Mol. Biol. 12, 915-922.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 915-922
    • Fukunaga, R.1    Yokoyama, S.2
  • 16
    • 33644748247 scopus 로고    scopus 로고
    • Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with met and ile reveal a lock-and-key mechanism for amino acid discrimination
    • Liu, Y., Liao, J., Zhu, B., Wang, E. D., and Ding, J. (2006) Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with met and ile reveal a lock-and-key mechanism for amino acid discrimination, Biochem. J. 394, 399-407.
    • (2006) Biochem. J , vol.394 , pp. 399-407
    • Liu, Y.1    Liao, J.2    Zhu, B.3    Wang, E.D.4    Ding, J.5
  • 17
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-Model and the Swiss-Pdbviewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) Swiss-Model and the Swiss-Pdbviewer: an environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 18
    • 0031301321 scopus 로고    scopus 로고
    • Non-standard amino acid recognition by Escherichia coli leucyl-tRNA synthetase
    • Martinis, S. A., and Fox, G. E. (1997) Non-standard amino acid recognition by Escherichia coli leucyl-tRNA synthetase, Nucleic Acids Symp. Ser. 36, 125-128.
    • (1997) Nucleic Acids Symp. Ser , vol.36 , pp. 125-128
    • Martinis, S.A.1    Fox, G.E.2
  • 19
    • 28244498723 scopus 로고    scopus 로고
    • Two conserved threonines collaborate in the Escherichia coli leucyl-tRNA synthetase amino acid editing mechanism
    • Zhai, Y., and Martinis, S. A. (2005) Two conserved threonines collaborate in the Escherichia coli leucyl-tRNA synthetase amino acid editing mechanism, Biochemistry 44, 15437-15443.
    • (2005) Biochemistry , vol.44 , pp. 15437-15443
    • Zhai, Y.1    Martinis, S.A.2
  • 20
    • 0023840230 scopus 로고
    • OmpT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg, J., and Dunn, J. J. (1988) OmpT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification, J. Bacteriol. 170, 1245-1253.
    • (1988) J. Bacteriol , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 21
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson, J. R., and Uhlenbeck, O. C. (1988) Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro, Proc. Natl. Acad. Sci. U.S.A. 85, 1033-1037.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 22
  • 24
    • 0037178055 scopus 로고    scopus 로고
    • Rational design to block amino acid editing of a tRNA synthetase
    • Mursinna, R. S., and Martinis, S. A. (2002) Rational design to block amino acid editing of a tRNA synthetase, J. Am. Chem. Soc. 124, 7286-7287.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 7286-7287
    • Mursinna, R.S.1    Martinis, S.A.2
  • 25
    • 0015522966 scopus 로고
    • Transfer ribonucleic acid synthetase catalyzed deacylation of aminoacyl transfer ribonucleic acid in the absence of adenosine monophosphate and pyrophosphate
    • Schreier, A. A., and Schimmel, P. R. (1972) Transfer ribonucleic acid synthetase catalyzed deacylation of aminoacyl transfer ribonucleic acid in the absence of adenosine monophosphate and pyrophosphate, Biochemistry 11, 1582-1589.
    • (1972) Biochemistry , vol.11 , pp. 1582-1589
    • Schreier, A.A.1    Schimmel, P.R.2
  • 26
    • 0038345361 scopus 로고    scopus 로고
    • The tRNA synthetase proofreading and editing active site: A novel antibiotic drug, in SAAS
    • Ballal, S. K, Ed, SAAS, Cookeville, TN
    • Lincecum, T. L., Jr., and Martinis, S. A. (2000) The tRNA synthetase proofreading and editing active site: a novel antibiotic drug, in SAAS Bulletin Biochemistry and Biotechnology (Ballal, S. K., Ed.) Vol. 13, pp 25-33, SAAS, Cookeville, TN.
    • (2000) Bulletin Biochemistry and Biotechnology , vol.13 , pp. 25-33
    • Lincecum Jr., T.L.1    Martinis, S.A.2
  • 27
    • 0026059951 scopus 로고    scopus 로고
    • Mechulam, Y., Dardel, F., Le, Corre, D., Blanquet, S., and Fayat, G. (1991) Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase from Escherichia coli, J. Mol. Biol. 217, 465-475.
    • Mechulam, Y., Dardel, F., Le, Corre, D., Blanquet, S., and Fayat, G. (1991) Lysine 335, part of the KMSKS signature sequence, plays a crucial role in the amino acid activation catalysed by the methionyl-tRNA synthetase from Escherichia coli, J. Mol. Biol. 217, 465-475.
  • 28
    • 0028172539 scopus 로고
    • Methionyl-tRNA synthetase needs an intact and mobile 332KM-SKS336 motif in catalysis of methionyl adenylate formation
    • Schmitt, E., Meinnel, T., Blanquet, S., and Mechulam, Y. (1994) Methionyl-tRNA synthetase needs an intact and mobile 332KM-SKS336 motif in catalysis of methionyl adenylate formation, J. Mol. Biol. 242, 566-576.
    • (1994) J. Mol. Biol , vol.242 , pp. 566-576
    • Schmitt, E.1    Meinnel, T.2    Blanquet, S.3    Mechulam, Y.4
  • 29
    • 0028902065 scopus 로고
    • Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles
    • First, E. A., and Fersht, A. R. (1995) Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles, Biochemistry 34, 5030-5043.
    • (1995) Biochemistry , vol.34 , pp. 5030-5043
    • First, E.A.1    Fersht, A.R.2
  • 30
    • 0037273353 scopus 로고    scopus 로고
    • Mechanism of molecular interactions for tRNA(val) recognition by valyl-tRNA synthetase
    • Fukai, S., Nureki, O., Sekine, S., Shimada, A., Vassylyev, D. G., and Yokoyama, S. (2003) Mechanism of molecular interactions for tRNA(val) recognition by valyl-tRNA synthetase, RNA 9, 100-111.
    • (2003) RNA , vol.9 , pp. 100-111
    • Fukai, S.1    Nureki, O.2    Sekine, S.3    Shimada, A.4    Vassylyev, D.G.5    Yokoyama, S.6
  • 31
    • 0034703763 scopus 로고    scopus 로고
    • Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase
    • Fukai, S., Nureki, O., Sekine, S., Shimada, A., Tao, J., Vassylyev, D. G., and Yokoyama, S. (2000) Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase, Cell 103, 793-803.
    • (2000) Cell , vol.103 , pp. 793-803
    • Fukai, S.1    Nureki, O.2    Sekine, S.3    Shimada, A.4    Tao, J.5    Vassylyev, D.G.6    Yokoyama, S.7
  • 32
    • 1542376205 scopus 로고    scopus 로고
    • Molecular modeling study of the editing active site of Escherichia coli leucyl-tRNA synthetase: Two amino acid binding sites in the editing domain
    • Lee, K. W., and Briggs, J. M. (2004) Molecular modeling study of the editing active site of Escherichia coli leucyl-tRNA synthetase: two amino acid binding sites in the editing domain, Proteins 54, 693-704.
    • (2004) Proteins , vol.54 , pp. 693-704
    • Lee, K.W.1    Briggs, J.M.2
  • 33
    • 0022467280 scopus 로고
    • Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3′-end of tRNA
    • Hountondji, C., Lederer, F., Dessen, P., and Blanquet, S. (1986) Escherichia coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3′-end of tRNA, Biochemistry 25, 16-21.
    • (1986) Biochemistry , vol.25 , pp. 16-21
    • Hountondji, C.1    Lederer, F.2    Dessen, P.3    Blanquet, S.4
  • 35
    • 0034681169 scopus 로고    scopus 로고
    • The "KMSKS" motif in tyrosyl-tRNA synthetase participates in the initial binding of tRNA(Tyr)
    • 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.
    • (2000) Biochemistry , vol.39 , pp. 340-347
    • Xin, Y.1    Li, W.2    First, E.A.3
  • 36
    • 12344283963 scopus 로고    scopus 로고
    • Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase
    • Kobayashi, T., Takimura, T., Sekine, R., Kelly, V. P., Kamata, K., Sakamoto, K., Nishimura, S., and Yokoyama, S. (2005) Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase, J. Mol. Biol. 346, 105-117.
    • (2005) J. Mol. Biol , vol.346 , pp. 105-117
    • Kobayashi, T.1    Takimura, T.2    Sekine, R.3    Kelly, V.P.4    Kamata, K.5    Sakamoto, K.6    Nishimura, S.7    Yokoyama, S.8
  • 37
    • 0037099498 scopus 로고    scopus 로고
    • Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition
    • Yaremchuk, A., Kriklivyi, I., Tukalo, M., and Cusack, S. (2002) Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition, EMBO J. 21, 3829-3840.
    • (2002) EMBO J , vol.21 , pp. 3829-3840
    • Yaremchuk, A.1    Kriklivyi, I.2    Tukalo, M.3    Cusack, S.4
  • 38
    • 0027872349 scopus 로고
    • The SKS of the KMSKS signature of class I aminoacyl-tRNA synthetases corresponds to the GKT/S sequence characteristic of the ATP-binding site of many proteins
    • Hountondji, C., Dessen, P., and Blanquet, S. (1993) The SKS of the KMSKS signature of class I aminoacyl-tRNA synthetases corresponds to the GKT/S sequence characteristic of the ATP-binding site of many proteins, Biochimie 75, 1137-1142.
    • (1993) Biochimie , vol.75 , pp. 1137-1142
    • Hountondji, C.1    Dessen, P.2    Blanquet, S.3
  • 39
    • 0037126707 scopus 로고    scopus 로고
    • Crucial role of conserved lysine 277 in the fidelity of tRNA aminoacylation by Escherichia coli valyl-tRNA synthetase
    • Hountondji, C., Lazennec, C., Beauvallet, C., Dessen, P., Pernollet, J. C., Plateau, P., and Blanquet, S. (2002) Crucial role of conserved lysine 277 in the fidelity of tRNA aminoacylation by Escherichia coli valyl-tRNA synthetase, Biochemistry 41, 14856-14865.
    • (2002) Biochemistry , vol.41 , pp. 14856-14865
    • Hountondji, C.1    Lazennec, C.2    Beauvallet, C.3    Dessen, P.4    Pernollet, J.C.5    Plateau, P.6    Blanquet, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.