메뉴 건너뛰기




Volumn 46, Issue 11, 2007, Pages 3331-3337

Modulation of substrate specificity within the amino acid editing site of leucyl-tRNA synthetase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BIOSYNTHESIS; ESCHERICHIA COLI; RNA;

EID: 33947412310     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061778l     Document Type: Article
Times cited : (8)

References (29)
  • 1
    • 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
  • 2
    • 0032729798 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: A new image for a classical family
    • Martinis, S. A., Plateau, P., Cavarelli, J., and Florentz, C. (1999) Aminoacyl-tRNA synthetases: a new image for a classical family, Biochimie 81, 683-700.
    • (1999) Biochimie , vol.81 , pp. 683-700
    • Martinis, S.A.1    Plateau, P.2    Cavarelli, J.3    Florentz, C.4
  • 3
    • 2342431929 scopus 로고    scopus 로고
    • Transfer RNA-dependent amino acid discrimination by aminoacyl-tRNA synthetases
    • LaPointe, J, and Brakier-Gingras, L, Eds, pp, Klumer Academic/Plenum Publishers, New York
    • Hendrickson, T. L., and Schimmel, P. (2003) Transfer RNA-dependent amino acid discrimination by aminoacyl-tRNA synthetases, in Translation Mechanisms (LaPointe, J., and Brakier-Gingras, L., Eds.) pp 34-64, Klumer Academic/Plenum Publishers, New York.
    • (2003) Translation Mechanisms , pp. 34-64
    • Hendrickson, T.L.1    Schimmel, P.2
  • 4
    • 0017326738 scopus 로고
    • Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase
    • Fersht, A. R. (1977) Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase, Biochemistry 16, 1025-1030.
    • (1977) Biochemistry , vol.16 , pp. 1025-1030
    • Fersht, A.R.1
  • 5
    • 0032562707 scopus 로고    scopus 로고
    • Sieves in sequence
    • Fersht, A. R. (1998) Sieves in sequence, Science 280, 541.
    • (1998) Science , vol.280 , pp. 541
    • Fersht, A.R.1
  • 6
    • 0018788756 scopus 로고
    • Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases
    • Fersht, A. R., and Dingwall, C. (1979) Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases, Biochemistry 18, 2627-2631.
    • (1979) Biochemistry , vol.18 , pp. 2627-2631
    • Fersht, A.R.1    Dingwall, C.2
  • 7
    • 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
  • 10
    • 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
  • 11
    • 0029854940 scopus 로고    scopus 로고
    • Aminoacylation error correction
    • Lin, L., Hale, S. P., and Schimmel, P. (1996) Aminoacylation error correction, Nature 384, 33-34.
    • (1996) Nature , vol.384 , pp. 33-34
    • Lin, L.1    Hale, S.P.2    Schimmel, P.3
  • 13
    • 0037154266 scopus 로고    scopus 로고
    • Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase
    • Bishop, A. C., Nomanbhoy, T. K., and Schimmel, P. (2002) Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase, Proc. Natl. Acad. Sci. U.S.A. 99, 585-590.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 585-590
    • Bishop, A.C.1    Nomanbhoy, T.K.2    Schimmel, P.3
  • 15
    • 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
  • 16
    • 0346096859 scopus 로고    scopus 로고
    • Molecular dissection of a critical specificity determinant within the amino acid editing domain of leucyl-tRNA synthetase
    • Mursinna, R. S., Lee, K. W., Briggs, J. M., and Martinis, S. A. (2004) Molecular dissection of a critical specificity determinant within the amino acid editing domain of leucyl-tRNA synthetase, Biochemistry 43, 155-165.
    • (2004) Biochemistry , vol.43 , pp. 155-165
    • Mursinna, R.S.1    Lee, K.W.2    Briggs, J.M.3    Martinis, S.A.4
  • 17
    • 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
  • 18
    • 0037183472 scopus 로고    scopus 로고
    • Attenuation of the editing activity of the Escherichia coli leucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo
    • Tang, Y., and Tirrell, D. A. (2002) Attenuation of the editing activity of the Escherichia coli leucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo, Biochemistry 41, 10635-10645.
    • (2002) Biochemistry , vol.41 , pp. 10635-10645
    • Tang, Y.1    Tirrell, D.A.2
  • 20
    • 0028233381 scopus 로고
    • RNA template-directed RNA synthesis by T7 RNA polymerase
    • Cazenave, C., and Uhlenbeck, O. C. (1994) RNA template-directed RNA synthesis by T7 RNA polymerase, Proc. Natl. Acad. Sci. U.S.A. 91, 6972-6976.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 6972-6976
    • Cazenave, C.1    Uhlenbeck, O.C.2
  • 21
    • 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
  • 22
    • 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
  • 24
    • 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
  • 25
    • 0035788034 scopus 로고    scopus 로고
    • Formation of two classes of tRNA synthetases in relation to editing functions and genetic code
    • Schimmel, P., and Ribas de Pouplana, L. (2001) Formation of two classes of tRNA synthetases in relation to editing functions and genetic code, Cold Spring Harb Symp. Quant. Biol. 66, 161-166.
    • (2001) Cold Spring Harb Symp. Quant. Biol , vol.66 , pp. 161-166
    • Schimmel, P.1    Ribas de Pouplana, L.2
  • 26
    • 1542349267 scopus 로고    scopus 로고
    • Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine
    • Fukunaga, R., Fukai, S., Ishitani, R., Nureki, O., and Yokoyama, S. (2004) Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine, J. Biol. Chem. 279, 8396-8402.
    • (2004) J. Biol. Chem , vol.279 , pp. 8396-8402
    • Fukunaga, R.1    Fukai, S.2    Ishitani, R.3    Nureki, O.4    Yokoyama, S.5
  • 27
    • 33744899308 scopus 로고    scopus 로고
    • Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase
    • Fukunaga, R., and Yokoyama, S. (2006) Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase, J. Mol. Biol. 359, 901-912.
    • (2006) J. Mol. Biol , vol.359 , pp. 901-912
    • Fukunaga, R.1    Yokoyama, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.