메뉴 건너뛰기




Volumn 41, Issue 3, 2013, Pages 1859-1872

Crucial role of the C-terminal domain of Mycobacterium tuberculosis leucyl-tRNA synthetase in aminoacylation and editing

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; LEUCINE TRANSFER RNA LIGASE; TRANSFER RNA; VALINE;

EID: 84873690898     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks1307     Document Type: Article
Times cited : (14)

References (54)
  • 1
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases the genetic code, and the evolutionary process
    • Woese,C.R., Olsen,G.J., Ibba,M. and So? ll,D. (2000) Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol. Mol. Biol. Rev., 64, 202-236.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 202-236
    • Ibba, M.1    Soll, D.2
  • 2
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba,M. and So? ll,D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem., 69, 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 3
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani,G., Delarue,M., Poch,O., Gangloff,J. and Moras,D. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature, 347, 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Gangloff, J.1    Moras, D.2
  • 4
    • 0025874160 scopus 로고
    • Sequence, structural and evolutionary relationships between Class 2 aminoacyl-tRNA synthetases
    • Cusack,S., Ha? rtlein,M. and Leberman,R. (1991) Sequence, structural and evolutionary relationships between Class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res., 19, 3489-3498.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3489-3498
    • Cusack, S.1    Hartlein, M.2    Leberman, R.3
  • 5
    • 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
  • 6
    • 0015378783 scopus 로고
    • The frequency of errors in protein biosynthesis
    • Loftfield,R.B. and Vanderjagt,D. (1972) The frequency of errors in protein biosynthesis. Biochem. J., 128, 1353-1356.
    • (1972) Biochem. J. , vol.128 , pp. 1353-1356
    • Loftfield, R.B.1    Vanderjagt, D.2
  • 7
    • 0026795220 scopus 로고
    • Editing of errors in selection of amino acids for protein synthesis
    • Jakubowski,H. and Goldman,E. (1992) Editing of errors in selection of amino acids for protein synthesis. Microbiol. Rev., 56, 412-429.
    • (1992) Microbiol. Rev. , vol.56 , pp. 412-429
    • Jakubowski, H.1    Goldman, E.2
  • 8
    • 0040559883 scopus 로고    scopus 로고
    • Quality control mechanisms during translation
    • Ibba,M. and So? ll,D. (1999) Quality control mechanisms during translation. Science, 286, 1893-1897.
    • (1999) Science , vol.286 , pp. 1893-1897
    • Ibba, M.1    Soll, D.2
  • 9
    • 70349545940 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis and translational quality control
    • Ling,J.Q., Reynolds,N. and Ibba,M. (2009) Aminoacyl-tRNA synthesis and translational quality control. Annu. Rev. Microbiol., 63, 61-78.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 61-78
    • Reynolds, N.1    Ibba, M.2
  • 10
    • 42349103482 scopus 로고    scopus 로고
    • Fidelity mechanisms of the aminoacyl-tRNA synthetases
    • RajBhandary,U.L. and Ko? hrer,C. (eds 22, Springer- Verlag, Berlin Heidelberg
    • Mascarenhas,A.P., An,S., Rosen,A.E., Martinis,S.A. and Musier-Forsyth,K. (2009) Fidelity mechanisms of the aminoacyl-tRNA synthetases. In: RajBhandary,U.L. and Ko? hrer,C. (eds), Protein Engineering, Vol. 22, Springer-Verlag, Berlin Heidelberg, pp. 155-203.
    • (2009) Protein Engineering , pp. 155-203
    • Martinis, S.A.1    Musier-Forsyth, K.2
  • 11
    • 0034612210 scopus 로고    scopus 로고
    • CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function
    • Chen,J.F., Guo,N.N., Li,T., Wang,E.D. and Wang,Y.L. (2000) CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function. Biochemistry, 39, 6726-6731.
    • (2000) Biochemistry , vol.39 , pp. 6726-6731
    • Wang, E.D.1    Wang, Y.L.2
  • 12
    • 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
  • 13
    • 0014027087 scopus 로고
    • Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase
    • Baldwin,A.N. and Berg,P. (1966) Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase. J. Biol. Chem., 241, 839-845.
    • (1966) J. Biol. Chem. , vol.241 , pp. 839-845
    • Baldwin, A.N.1    Berg, P.2
  • 14
    • 0017072607 scopus 로고
    • Enzyme hyperspecificity Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
    • Fersht,A.R. and Kaethner,M.M. (1976) Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing. Biochemistry, 15, 3342-3346.
    • (1976) Biochemistry , vol.15 , pp. 3342-3346
    • Fersht, A.R.1    Kaethner, M.M.2
  • 15
    • 77449099886 scopus 로고    scopus 로고
    • TRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase
    • Tan,M., Zhu,B., Zhou,X.L., He,R., Chen,X., Eriani,G. and Wang,E.D. (2010) tRNA-dependent pre-transfer editing by prokaryotic leucyl-tRNA synthetase. J. Biol. Chem., 285, 3235-3244.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3235-3244
    • Eriani, G.1    Wang, E.D.2
  • 16
    • 0031000512 scopus 로고    scopus 로고
    • Discrete determinants in transfer RNA for editing and aminoacylation
    • Hale,S.P., Auld,D.S., Schmidt,E. and Schimmel,P. (1997) Discrete determinants in transfer RNA for editing and aminoacylation. Science, 276, 1250-1252.
    • (1997) Science , vol.276 , pp. 1250-1252
    • Schmidt, E.1    Schimmel, P.2
  • 17
    • 0032582796 scopus 로고    scopus 로고
    • In vitro selection of RNAs aminoacylated by Escherichia coli leucyl-tRNA synthetase
    • Asahara,H., Nameki,N. and Hasegawa,T. (1998) In vitro selection of RNAs aminoacylated by Escherichia coli leucyl-tRNA synthetase. J. Mol. Biol., 283, 605-618.
    • (1998) J. Mol. Biol. , vol.283 , pp. 605-618
    • Nameki, N.1    Hasegawa, T.2
  • 18
    • 0037052929 scopus 로고    scopus 로고
    • Identification of essential domains for Escherichia coli tRNALeu aminoacylation and amino acid editing using minimalist RNA molecules
    • Larkin,D.C., Williams,A.M., Martinis,S.A. and Fox,G.E. (2002) Identification of essential domains for Escherichia coli tRNALeu aminoacylation and amino acid editing using minimalist RNA molecules. Nucleic Acids Res., 30, 2103-2113.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2103-2113
    • Martinis, S.A.1    Fox, G.E.2
  • 19
    • 0038268059 scopus 로고    scopus 로고
    • Tertiary structure base pairs between D- and TcC-loops of Escherichia coli tRNALeu play important roles in both aminoacylation and editing
    • Du,X. and Wang,E.D. (2003) Tertiary structure base pairs between D- and TcC-loops of Escherichia coli tRNALeu play important roles in both aminoacylation and editing. Nucleic Acids Res., 31, 2865-2872.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2865-2872
    • Wang, E.D.1
  • 20
    • 80455178748 scopus 로고    scopus 로고
    • Role of tRNA amino acid-accepting end in aminoacylation and its quality control
    • Zhou,X.L., Du,D.H., Tan,M., Lei,H.Y., Ruan,L.L., Eriani,G. and Wang,E.D. (2011) Role of tRNA amino acid-accepting end in aminoacylation and its quality control. Nucleic Acids Res., 39, 8857-8868.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 8857-8868
    • Eriani, G.1    Wang, E.D.2
  • 21
    • 27144477810 scopus 로고    scopus 로고
    • The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation
    • Tukalo,M., Yaremchuk,A., Fukunaga,R., Yokoyama,S. and Cusack,S. (2005) The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation. Nat. Struct. Mol. Biol., 12, 923-930.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 923-930
    • Yokoyama, S.1    Cusack, S.2
  • 22
    • 84863723708 scopus 로고    scopus 로고
    • Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase
    • Palencia,A., Crepin,T., Vu,M.T., Lincecum,T.L. Jr, Martinis,S.A. and Cusack,S. (2012) Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase. Nat. Struct. Mol. Biol., 19, 677-684.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 677-684
    • Lincecum Jr., T.L.1    Martinis, S.A.2    Cusack, S.3
  • 23
    • 2942670336 scopus 로고    scopus 로고
    • Two distinct domains of the beta 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 beta 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
    • Eriani, G.1    Wang, E.D.2
  • 24
    • 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., Vannella,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
    • Vannella, K.M.1    Martinis, S.A.2
  • 25
    • 77952542701 scopus 로고    scopus 로고
    • Multidrug-resistant and extensively drug-resistant tuberculosis: A threat to global control of tuberculosis
    • Gandhi,N.R., Nunn,P., Dheda,K., Schaaf,H.S., Zignol,M., van Soolingen,D., Jensen,P. and Bayona,J. (2010) Multidrug-resistant and extensively drug-resistant tuberculosis: a threat to global control of tuberculosis. Lancet, 375, 1830-1843.
    • (2010) Lancet , vol.375 , pp. 1830-1843
    • Van Soolingen, D.1    Jensen, P.2    Bayona, J.3
  • 26
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole,S.T., Brosch,R., Parkhill,J., Garnier,T., Churcher,C., Harris,D., Gordon,S.V., Eiglmeier,K., Gas,S., Barry,C.E. 3rd et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature, 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Barry Iii, C.E.1
  • 27
    • 0033551859 scopus 로고    scopus 로고
    • Insights into editing from an Ile-tRNA synthetase structure with tRNAIle and mupirocin
    • Silvian,L.F., Wang,J. and Steitz,T.A. (1999) Insights into editing from an Ile-tRNA synthetase structure with tRNAIle and mupirocin. Science, 285, 1074-1077.
    • (1999) Science , vol.285 , pp. 1074-1077
    • Wang, J.1    Steitz, T.A.2
  • 29
    • 59749087749 scopus 로고    scopus 로고
    • Inhibition of methionyl-tRNA synthetase by REP8839 and effects of resistance mutations on enzyme activity
    • Green,L.S., Bullard,J.M., Ribble,W., Dean,F., Ayers,D.F., Ochsner,U.A., Janjic,N. and Jarvis,T.C. (2009) Inhibition of methionyl-tRNA synthetase by REP8839 and effects of resistance mutations on enzyme activity. Antimicrob. Agents Chemother., 53, 86-94.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 86-94
    • Janjic, N.1    Jarvis, T.C.2
  • 30
    • 77955903018 scopus 로고    scopus 로고
    • Discovery of novel benzoxaborole-based potent antitrypanosomal agents
    • Ding,D.Z., Zhao,Y.X., Meng,Q.Q., Xie,D.S., Nare,B., Chen,D.T., Bacchi,C.J., Yarlett,N., Zhang,Y.K., Hernandez,V. et al. (2010) Discovery of novel benzoxaborole-based potent antitrypanosomal agents. Acs. Med. Chem. Lett., 1, 165-169.
    • (2010) Acs. Med. Chem. Lett. , vol.1 , pp. 165-169
    • Hernandez, V.1
  • 31
    • 80054882325 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase inhibitors as potential antibiotics
    • Vondenhoff,G.H. and Van Aerschot,A. (2011) Aminoacyl-tRNA synthetase inhibitors as potential antibiotics. Eur. J. Med. Chem., 46, 5227-5236.
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 5227-5236
    • Vondenhoff, G.H.1    Van Aerschot, A.2
  • 32
    • 1542631893 scopus 로고    scopus 로고
    • Overproduction and purification of Escherichia coli tRNALeu
    • Li,Y., Wang,E.D. and Wang,Y.L. (1998) Overproduction and purification of Escherichia coli tRNALeu. Sci. China, C, Life Sci., 41, 225-231.
    • (1998) Sci. China C, Life Sci. , vol.41 , pp. 225-231
    • Wang, E.D.1    Wang, Y.L.2
  • 34
    • 21244439199 scopus 로고    scopus 로고
    • TRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class i aminoacyl-tRNA synthetase
    • Gruic-Sovulj,I., Uter,N., Bullock,T. and Perona,J.J. (2005) tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase. J. Biol. Chem., 280, 23978-23986.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23978-23986
    • Bullock, T.1    Perona, J.J.2
  • 35
    • 84859451220 scopus 로고    scopus 로고
    • A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity
    • Tan,M., Yan,W., Liu,R.J., Wang,M., Chen,X., Zhou,X.L. and Wang,E.D. (2012) A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity. Biochem J., 443, 477-484.
    • (2012) Biochem J. , vol.443 , pp. 477-484
    • Zhou, X.L.1    Wang, E.D.2
  • 36
    • 0029776689 scopus 로고    scopus 로고
    • A three-hybrid system to detect RNA-protein interactions in vivo
    • SenGupta,D.J., Zhang,B.L., Kraemer,B., Pochart,P., Fields,S. and Wickens,M. (1996) A three-hybrid system to detect RNA-protein interactions in vivo. Proc. Natl Acad. Sci. USA, 93, 8496-8501.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8496-8501
    • Fields, S.1    Wickens, M.2
  • 37
    • 63649123391 scopus 로고    scopus 로고
    • TRNA-independent pretransfer editing by class i leucyl-tRNA synthetase
    • Zhu,B., Yao,P., Tan,M., Eriani,G. and Wang,E.D. (2009) tRNA-independent pretransfer editing by class I leucyl-tRNA synthetase. J. Biol. Chem., 284, 3418-3424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3418-3424
    • Eriani, G.1    Wang, E.D.2
  • 38
    • 78651286311 scopus 로고    scopus 로고
    • Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase
    • Chen,X., Ma,J.J., Tan,M., Yao,P., Hu,Q.H., Eriani,G. and Wang,E.D. (2011) Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase. Nucleic Acids Res., 39, 235-247.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 235-247
    • Eriani, G.1    Wang, E.D.2
  • 39
    • 38349090724 scopus 로고    scopus 로고
    • A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases
    • Hsu,J.L. and Martinis,S.A. (2008) A Flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases. J. Mol. Biol., 376, 482-491.
    • (2008) J. Mol. Biol. , vol.376 , pp. 482-491
    • Hsu, J.L.1    Martinis, S.A.2
  • 40
    • 0030058229 scopus 로고    scopus 로고
    • The C-terminal extension of yeast seryl-tRNA synthetase affects stability of the enzyme and its substrate affinity
    • Weygand-Durasevic,I., Lenhard,B., Filipic,S. and So? ll,D. (1996) The C-terminal extension of yeast seryl-tRNA synthetase affects stability of the enzyme and its substrate affinity. J. Biol. Chem., 271, 2455-2461.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2455-2461
    • Filipic, S.1    Soll, D.2
  • 41
    • 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
  • 42
    • 27144445976 scopus 로고    scopus 로고
    • The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex
    • Ling,C., Yao,Y.N., Zheng,Y.G., Wei,H., Wang,L., Wu,X.F. and Wang,E.D. (2005) The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. J. Biol. Chem., 280, 34755-34763.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34755-34763
    • Wang, E.D.1
  • 43
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo,M., Yang,X.L. and Schimmel,P. (2010) New functions of aminoacyl-tRNA synthetases beyond translation. Nat. Rev. Mol. Cell Biol., 11, 668-674.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 668-674
    • Yang, X.L.1    Schimmel, P.2
  • 44
    • 0034703763 scopus 로고    scopus 로고
    • Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNAVal 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 tRNAVal and valyl-tRNA synthetase. Cell, 103, 793-803.
    • (2000) Cell , vol.103 , pp. 793-803
    • Vassylyev, D.G.1    Yokoyama, S.2
  • 45
    • 0029982470 scopus 로고    scopus 로고
    • A tRNA identity switch mediated by the binding interaction between a tRNA anticodon and the accessory domain of a class II aminoacyl-tRNA synthetase
    • Yan,W., Augustine,J. and Francklyn,C. (1996) A tRNA identity switch mediated by the binding interaction between a tRNA anticodon and the accessory domain of a class II aminoacyl-tRNA synthetase. Biochemistry, 35, 6559-6568.
    • (1996) Biochemistry , vol.35 , pp. 6559-6568
    • Augustine, J.1    Francklyn, C.2
  • 46
    • 0033550199 scopus 로고    scopus 로고
    • Unique recognition style of tRNALeu by Haloferax volcanii leucyl-tRNA synthetase
    • Soma,A., Uchiyama,K., Sakamoto,T., Maeda,M. and Himeno,H. (1999) Unique recognition style of tRNALeu by Haloferax volcanii leucyl-tRNA synthetase. J. Mol. Biol., 293, 1029-1038.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1029-1038
    • Maeda, M.1    Himeno, H.2
  • 47
    • 0028105601 scopus 로고
    • The 2.9 A ̊ crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer
    • Biou,V., Yaremchuk,A., Tukalo,M. and Cusack,S. (1994) The 2.9 A ̊ crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNASer. Science, 263, 1404-1410.
    • (1994) Science , vol.263 , pp. 1404-1410
    • Tukalo, M.1    Cusack, S.2
  • 48
    • 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
    • Tukalo, M.1    Cusack, S.2
  • 49
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki,N. and Tawfik,D.S. (2009) Protein dynamism and evolvability. Science, 324, 203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 50
    • 79952776436 scopus 로고    scopus 로고
    • WHO Global Tuberculosis Control Repor T. 2010 Summary
    • WHO global tuberculosis control report. (2010) Summary. Cent. Eur. J. Public Health, 18, 237.
    • Cent. Eur. J. Public Health , vol.18 , pp. 237
  • 51
    • 84870152928 scopus 로고    scopus 로고
    • Biosynthesis and function of posttranscriptional modifications of transfer RNAs
    • El Yacoubi,B., Bailly,M. and de Crécy-Lagard,V. (2012) Biosynthesis and function of posttranscriptional modifications of transfer RNAs. Annu. Rev. Genet., 46, 69-95.
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 69-95
    • El Yacoubi, B.1    Bailly, M.2    De Crécy-Lagard, V.3
  • 53
    • 67349127495 scopus 로고    scopus 로고
    • Crystal structures of the human and fungal cytosolic leucyl-tRNA synthetase editing domains: A structural basis for the rational design of antifungal benzoxaboroles
    • Seiradake,E., Mao,W., Hernandez,V., Baker,S.J., Plattner,J.J., Alley,M.R.K. and Cusack,S. (2009) Crystal structures of the human and fungal cytosolic leucyl-tRNA synthetase editing domains: a structural basis for the rational design of antifungal benzoxaboroles. J. Mol. Biol., 390, 196-207.
    • (2009) J. Mol. Biol. , vol.390 , pp. 196-207
    • Seiradake, E.1    Mao, W.2    Hernandez, V.3    Baker, S.J.4    Plattner, J.J.5    Alley, M.R.K.6    Cusack, S.7
  • 54
    • 14344250347 scopus 로고    scopus 로고
    • An aminoacyl-tRNA synthetase with a defunct editing site
    • Lue,S.W. and Kelley,S.O. (2005) An aminoacyl-tRNA synthetase with a defunct editing site. Biochemistry, 44, 3010-3016.
    • (2005) Biochemistry , vol.44 , pp. 3010-3016
    • Lue, S.W.1    Kelley, S.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.