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Volumn 41, Issue 9, 2013, Pages 4988-4998

Leucine-specific domain modulates the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GLYCYLLYSYLASPARTYLGLYCINE; LEUCINE; LEUCINE TRANSFER RNA LIGASE; TETRAPEPTIDE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84877299352     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt185     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 70349545940 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis and translational quality control
    • Ling, J., 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
    • Ling, J.1    Reynolds, N.2    Ibba, M.3
  • 2
    • 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
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 3
    • 0034657687 scopus 로고    scopus 로고
    • The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue
    • Cusack, S., Yaremchuk, A. and Tukalo, M. (2000) The 2 A 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
  • 4
    • 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
    • Palencia, A.1    Crepin, T.2    Vu, M.T.3    Lincecum Jr., T.L.4    Martinis, S.A.5    Cusack, S.6
  • 6
    • 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
  • 7
    • 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
  • 8
    • 34247581696 scopus 로고    scopus 로고
    • A unique insert of leucyl-tRNA synthetase is required for aminoacylation and not amino acid editing
    • Vu, M.T. and Martinis, S.A. (2007) A unique insert of leucyl-tRNA synthetase is required for aminoacylation and not amino acid editing. Biochemistry, 46, 5170-5176.
    • (2007) Biochemistry , vol.46 , pp. 5170-5176
    • Vu, M.T.1    Martinis, S.A.2
  • 9
    • 33845415567 scopus 로고    scopus 로고
    • Split leucine-specific domain of leucyl-tRNA synthetase from the hyperthermophilic bacterium Aquifex aeolicus
    • Ma, J.J., Zhao, M.W. and Wang, E.D. (2006) Split leucine-specific domain of leucyl-tRNA synthetase from the hyperthermophilic bacterium Aquifex aeolicus. Biochemistry, 45, 14809-14816.
    • (2006) Biochemistry , vol.45 , pp. 14809-14816
    • Ma, J.J.1    Zhao, M.W.2    Wang, E.D.3
  • 10
    • 79959348607 scopus 로고    scopus 로고
    • Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites
    • Li, L., Boniecki, M.T., Jaffe, J.D., Imai, B.S., Yau, P.M., Luthey-Schulten, Z.A. and Martinis, S.A. (2011) Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites. Proc. Natl Acad. Sci. USA, 108, 9378-9383.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9378-9383
    • Li, L.1    Boniecki, M.T.2    Jaffe, J.D.3    Imai, B.S.4    Yau, P.M.5    Luthey-Schulten, Z.A.6    Martinis, S.A.7
  • 11
    • 84870867839 scopus 로고    scopus 로고
    • Inter-domain communication modulates the tRNA-dependent pre-transfer editing of leucyl-tRNA synthetase
    • Tan, M., Zhu, B., Liu, R.J., Chen, X., Zhou, X.L. and Wang, E.D. (2013) Inter-domain communication modulates the tRNA-dependent pre-transfer editing of leucyl-tRNA synthetase. Biochem. J., 449, 123-131.
    • (2013) Biochem. J. , vol.449 , pp. 123-131
    • Tan, M.1    Zhu, B.2    Liu, R.J.3    Chen, X.4    Zhou, X.L.5    Wang, E.D.6
  • 12
    • 0027244036 scopus 로고
    • Compilation of tRNA sequences and sequences of tRNA genes
    • Steinberg, S., Misch, A. and Sprinzl, M. (1993) Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res., 21, 3011-3015.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3011-3015
    • Steinberg, S.1    Misch, A.2    Sprinzl, M.3
  • 13
    • 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
    • Zhou, X.L.1    Du, D.H.2    Tan, M.3    Lei, H.Y.4    Ruan, L.L.5    Eriani, G.6    Wang, E.D.7
  • 14
    • 0038268059 scopus 로고    scopus 로고
    • Tertiary structure base pairs between D-and TpsiC-loops of Escherichia coli tRNA(Leu) play important roles in both aminoacylation and editing
    • Du, X. and Wang, E.D. (2003) Tertiary structure base pairs between D-and TpsiC-loops of Escherichia coli tRNA(Leu) play important roles in both aminoacylation and editing. Nucleic Acids Res., 31, 2865-2872.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2865-2872
    • Du, X.1    Wang, E.D.2
  • 15
    • 53049108811 scopus 로고    scopus 로고
    • Unique residues crucial for optimal editing in yeast cytoplasmic Leucyl-tRNA synthetase are revealed by using a novel knockout yeast strain
    • Yao, P., Zhou, X.L., He, R., Xue, M.Q., Zheng, Y.G., Wang, Y.F. and Wang, E.D. (2008) Unique residues crucial for optimal editing in yeast cytoplasmic Leucyl-tRNA synthetase are revealed by using a novel knockout yeast strain. J. Biol. Chem., 283, 22591-22600.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22591-22600
    • Yao, P.1    Zhou, X.L.2    He, R.3    Xue, M.Q.4    Zheng, Y.G.5    Wang, Y.F.6    Wang, E.D.7
  • 17
    • 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
    • Tan, M.1    Yan, W.2    Liu, R.J.3    Wang, M.4    Chen, X.5    Zhou, X.L.6    Wang, E.D.7
  • 18
    • 1542631893 scopus 로고    scopus 로고
    • Overproduction and purification of Escherichia coli tRNA(Leu)
    • Li, Y., Wang, E.D. and Wang, Y.L. (1998) Overproduction and purification of Escherichia coli tRNA(Leu). Sci. China C Life Sci., 41, 225-231.
    • (1998) Sci. China C Life Sci. , vol.41 , pp. 225-231
    • Li, Y.1    Wang, E.D.2    Wang, Y.L.3
  • 19
    • 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
    • Tan, M.1    Zhu, B.2    Zhou, X.L.3    He, R.4    Chen, X.5    Eriani, G.6    Wang, E.D.7
  • 20
    • 0024300362 scopus 로고
    • Changing the acceptor identity of a transfer RNA by altering nucleotides in a "variable pocket"
    • McClain, W.H. and Foss, K. (1988) Changing the acceptor identity of a transfer RNA by altering nucleotides in a "variable pocket". Science, 241, 1804-1807.
    • (1988) Science , vol.241 , pp. 1804-1807
    • McClain, W.H.1    Foss, K.2
  • 23
    • 0029009371 scopus 로고
    • Transfer RNA: From minihelix to genetic code
    • Schimmel, P. and Ribas de Pouplana, L. (1995) Transfer RNA: from minihelix to genetic code. Cell, 81, 983-986.
    • (1995) Cell , vol.81 , pp. 983-986
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 24
    • 0025990945 scopus 로고
    • Four sites in the acceptor helix and one site in the variable pocket of tRNA(Ala) determine the molecule's acceptor identity
    • McClain, W.H., Foss, K., Jenkins, R.A. and Schneider, J. (1991) Four sites in the acceptor helix and one site in the variable pocket of tRNA(Ala) determine the molecule's acceptor identity. Proc. Natl Acad. Sci. USA, 88, 9272-9276.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9272-9276
    • McClain, W.H.1    Foss, K.2    Jenkins, R.A.3    Schneider, J.4
  • 26
    • 0032737525 scopus 로고    scopus 로고
    • A single base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation
    • Liu, W., Huang, Y., Eriani, G., Gangloff, J., Wang, E. and Wang, Y. (1999) A single base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation. Biochim. Biophys. Acta, 1473, 356-362.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 356-362
    • Liu, W.1    Huang, Y.2    Eriani, G.3    Gangloff, J.4    Wang, E.5    Wang, Y.6
  • 27
    • 33847794900 scopus 로고    scopus 로고
    • Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain
    • SternJohn, J., Hati, S., Siliciano, P.G. and Musier-Forsyth, K. (2007) Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain. Proc. Natl Acad. Sci. USA, 104, 2127-2132.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2127-2132
    • Sternjohn, J.1    Hati, S.2    Siliciano, P.G.3    Musier-Forsyth, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.