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Volumn 188, Issue 1, 2006, Pages 269-274

Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE TRANSFER RNA; ASPARTATE TRANSFER RNA LIGASE; ASPARTIC ACID TRANSFER RNA; BACTERIAL ENZYME; GLYCINE; HISTIDINE; LEUCINE; LYSINE; NUCLEIC ACID BASE; TRANSFER RNA;

EID: 33644913721     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.1.269-274.2006     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 1642459148 scopus 로고    scopus 로고
    • Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1
    • Akochy, P. M., D. Bernard, P. H. Roy, and J. Lapointe. 2004. Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1. J. Bacteriol. 186:767-776.
    • (2004) J. Bacteriol. , vol.186 , pp. 767-776
    • Akochy, P.M.1    Bernard, D.2    Roy, P.H.3    Lapointe, J.4
  • 3
    • 0026503359 scopus 로고
    • A two-component T7 system for the overexpression of genes in Pseudomonas aeruginosa
    • Brunschwig, E., and A. Darzins. 1992. A two-component T7 system for the overexpression of genes in Pseudomonas aeruginosa. Gene 111:35-41.
    • (1992) Gene , vol.111 , pp. 35-41
    • Brunschwig, E.1    Darzins, A.2
  • 5
    • 0037390217 scopus 로고    scopus 로고
    • Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain
    • Charron, C., H. Roy, M. Blaise, R. Giege, and D. Kern. 2003. Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain. EMBO J. 22:1632-1643.
    • (2003) EMBO J. , vol.22 , pp. 1632-1643
    • Charron, C.1    Roy, H.2    Blaise, M.3    Giege, R.4    Kern, D.5
  • 7
    • 0029781454 scopus 로고    scopus 로고
    • RNA-dependent asparagine formation
    • Curnow, A. W., M. Ibba, and D. Soll. 1996. tRNA-dependent asparagine formation. Nature 382:589-590.
    • (1996) Nature , vol.382 , pp. 589-590
    • Curnow, A.W.1    Ibba, M.2    Soll, D.3
  • 9
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani, G., M. Delarue, O. Poch, J. Gangloff, and D. Moras. 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
  • 10
    • 0038286152 scopus 로고    scopus 로고
    • Expanding tRNA recognition of a tRNA synthetase by a single amino acid change
    • Feng, L., D. Tumbula-Hansen, H. Toogood, and D. Soil. 2003. Expanding tRNA recognition of a tRNA synthetase by a single amino acid change. Proc. Natl. Acad. Sci. USA 100:5676-5681.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5676-5681
    • Feng, L.1    Tumbula-Hansen, D.2    Toogood, H.3    Soil, D.4
  • 13
    • 0242723221 scopus 로고    scopus 로고
    • Transfer RNA structure and identity
    • J. Lapointe and L. Brakier-Gingras (ed.). Kluwer Academic/Plenum Publishers, New York, N.Y.
    • Giege, R., and M. Frugier. 2003. Transfer RNA structure and identity, p. 1-24. In J. Lapointe and L. Brakier-Gingras (ed.), Translation mechanisms. Kluwer Academic/Plenum Publishers, New York, N.Y.
    • (2003) Translation Mechanisms , pp. 1-24
    • Giege, R.1    Frugier, M.2
  • 14
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M., and D. Soll. 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
  • 15
    • 0034991910 scopus 로고    scopus 로고
    • The renaissance of aminoacyl-tRNA synthesis
    • Ibba, M., and D. Soll. 2001. The renaissance of aminoacyl-tRNA synthesis. EMBO Rep. 2:382-387.
    • (2001) EMBO Rep. , vol.2 , pp. 382-387
    • Ibba, M.1    Soll, D.2
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47(Pt. 2):110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 18
    • 0035956903 scopus 로고    scopus 로고
    • Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria
    • Kowal, A. K., C. Kohrer, and U. L. RajBhandary. 2001. Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria. Proc. Natl. Acad. Sci. USA 98:2268-2273.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2268-2273
    • Kowal, A.K.1    Kohrer, C.2    Rajbhandary, U.L.3
  • 19
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • LaRiviere, F. J., A. D. Wolfson, and O. C. Uhlenbeck. 2001. Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science 294:165-168.
    • (2001) Science , vol.294 , pp. 165-168
    • Lariviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 20
    • 33646549054 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1982)
    • Maniatis, T.1    Fritsch, E.F.2    Sambrook, J.3
  • 21
    • 3242890837 scopus 로고    scopus 로고
    • Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo
    • Martin, F., S. Barends, and G. Eriani. 2004. Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo. Nucleic Acids Res. 32:4081-4089.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4081-4089
    • Martin, F.1    Barends, S.2    Eriani, G.3
  • 22
  • 24
    • 0035824544 scopus 로고    scopus 로고
    • A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis
    • Raczniak, G., H. D. Becker, B. Min, and D. Soll. 2001. A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis. J. Biol. Chem. 276:45862-45867.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45862-45867
    • Raczniak, G.1    Becker, H.D.2    Min, B.3    Soll, D.4
  • 25
    • 0035816460 scopus 로고    scopus 로고
    • A dual-specific Glu-tRNA(Gln) and Asp-tRNA(Asn) amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans
    • Salazar, J. C., R. Zuniga, G. Raczniak, H. Becker, D. Soll, and O. Orellana. 2001. A dual-specific Glu-tRNA(Gln) and Asp-tRNA(Asn) amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans. FEBS Lett. 500:129-131.
    • (2001) FEBS Lett. , vol.500 , pp. 129-131
    • Salazar, J.C.1    Zuniga, R.2    Raczniak, G.3    Becker, H.4    Soll, D.5    Orellana, O.6
  • 27
    • 0024285823 scopus 로고
    • Protein biosynthesis in organelles requires misaminoacylation of tRNA
    • Schon, A., C. G. Kannangara, S. Gough, and D. Soll. 1988. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature 331:187-190.
    • (1988) Nature , vol.331 , pp. 187-190
    • Schon, A.1    Kannangara, C.G.2    Gough, S.3    Soll, D.4
  • 28
    • 33344461481 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase structure and evolution
    • J. Lapointe and L. Brakier-Gingras (ed.). Kluwer Academic/Plenum Publishers, New York, N.Y.
    • Soll, D., and M. Ibba. 2003. Aminoacyl-tRNA synthetase structure and evolution, p. 25-33. In J. Lapointe and L. Brakier-Gingras (ed.), Translation mechanisms. Kluwer Academic/Plenum Publishers, New York, N.Y.
    • (2003) Translation Mechanisms , pp. 25-33
    • Soll, D.1    Ibba, M.2
  • 29
    • 0027976415 scopus 로고
    • Discrimination against misacylated tRNA by chloroplast elongation factor Tu
    • Stanzel, M., A. Schon, and M. Sprinzl. 1994. Discrimination against misacylated tRNA by chloroplast elongation factor Tu. Eur. J. Biochem. 219:435-439.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 435-439
    • Stanzel, M.1    Schon, A.2    Sprinzl, M.3
  • 32
    • 0037020225 scopus 로고    scopus 로고
    • Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms
    • Tumbula-Hansen, D., L. Feng, H. Toogood, K. O. Stetter, and D. Soll. 2002. Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms. J. Biol. Chem. 277:37184-37190.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37184-37190
    • Tumbula-Hansen, D.1    Feng, L.2    Toogood, H.3    Stetter, K.O.4    Soll, D.5
  • 33
    • 0029947989 scopus 로고    scopus 로고
    • Construction of improved vectors for protein production in Pseudomonas aeruginosa
    • Watson, A. A., R. A. Alm, and J. S. Mattick. 1996. Construction of improved vectors for protein production in Pseudomonas aeruginosa. Gene 172:163-164.
    • (1996) Gene , vol.172 , pp. 163-164
    • Watson, A.A.1    Alm, R.A.2    Mattick, J.S.3
  • 34
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner, M. P., G. L. Costa, W. Schoettlin, J. Cline, E. Mathur, and J. C. Bauer. 1994. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151:119-123.
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 35
    • 0014324873 scopus 로고
    • Transfer RNA as a cofactor coupling amino acid synthesis with that of protein
    • Wilcox, M., and M. Nirenberg. 1968. Transfer RNA as a cofactor coupling amino acid synthesis with that of protein. Proc. Natl. Acad. Sci. USA 61:229-236.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 229-236
    • Wilcox, M.1    Nirenberg, M.2
  • 36
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process
    • Woese, C. R., G. J. Olsen, M. Ibba, and D. Soll. 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
    • Woese, C.R.1    Olsen, G.J.2    Ibba, M.3    Soll, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.