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Volumn 377, Issue 3, 2008, Pages 845-853

Methanothermobacter thermautotrophicus tRNAGln Confines the Amidotransferase GatCAB to Asparaginyl-tRNAAsn Formation

Author keywords

Asp AdT; GatCAB; GatDE; Glu AdT; tRNA dependent amidotransferase

Indexed keywords

AMIDE; AMINOTRANSFERASE; ASPARAGINE TRANSFER RNA; ENZYME GATCAB; ENZYME GATDE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 40649114689     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.064     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 0034618571 scopus 로고    scopus 로고
    • Domain-specific recruitment of amide amino acids for protein synthesis
    • D.L. Tumbula H.D. Becker W.Z. Chang D. Söll Domain-specific recruitment of amide amino acids for protein synthesis Nature 407 2000 106 110
    • (2000) Nature , vol.407 , pp. 106-110
    • Tumbula, D.L.1    Becker, H.D.2    Chang, W.Z.3    Söll, D.4
  • 2
    • 0042388199 scopus 로고    scopus 로고
    • When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism
    • H. Roy H.D. Becker J. Reinbolt D. Kern When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism Proc. Natl. Acad. Sci. USA 100 2003 9837 9842
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9837-9842
    • Roy, H.1    Becker, H.D.2    Reinbolt, J.3    Kern, D.4
  • 4
    • 0022449958 scopus 로고
    • A single glutamyl-tRNA synthetase aminoacylates tRNAGlu and tRNAGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNAGln1 in vitro
    • Gln1 in vitro J. Bacteriol. 165 1986 88 93
    • (1986) J. Bacteriol. , vol.165 , pp. 88-93
    • Lapointe, J.1    Duplain, L.2    Proulx, M.3
  • 5
    • 0014324873 scopus 로고
    • Transfer RNA as a cofactor coupling amino acid synthesis with that of protein
    • M. Wilcox M. Nirenberg Transfer RNA as a cofactor coupling amino acid synthesis with that of protein Proc. Natl. Acad. Sci. USA 61 1968 229 236
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 229-236
    • Wilcox, M.1    Nirenberg, M.2
  • 6
    • 0030811296 scopus 로고    scopus 로고
    • Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus. Structural and biochemical properties of the two enzymes
    • H.D. Becker J. Reinbolt R. Kreutzer R. Giege D. Kern Existence of two distinct aspartyl-tRNA synthetases in Thermus thermophilus . Structural and biochemical properties of the two enzymes Biochemistry 36 1997 8785 8797
    • (1997) Biochemistry , vol.36 , pp. 8785-8797
    • Becker, H.D.1    Reinbolt, J.2    Kreutzer, R.3    Giege, R.4    Kern, D.5
  • 7
    • 0029781454 scopus 로고    scopus 로고
    • tRNA-dependent asparagine formation
    • A.W. Curnow M. Ibba D. Söll tRNA-dependent asparagine formation Nature 382 1996 589 590
    • (1996) Nature , vol.382 , pp. 589-590
    • Curnow, A.W.1    Ibba, M.2    Söll, D.3
  • 8
    • 0032573150 scopus 로고    scopus 로고
    • Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways
    • H.D. Becker D. Kern Thermus thermophilus : a link in evolution of the tRNA-dependent amino acid amidation pathways Proc. Natl. Acad. Sci. USA 95 1998 12832 12837
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12832-12837
    • Becker, H.D.1    Kern, D.2
  • 10
    • 0014643835 scopus 로고
    • Gamma-phosphoryl ester of Glu-tRNAGln as an intermediate in Bacillus subtilis glutaminyl-tRNA synthesis
    • Gln as an intermediate in Bacillus subtilis glutaminyl-tRNA synthesis Cold Spring Harb. Symp. Quant. Biol. 34 1969 521 528
    • (1969) Cold Spring Harb. Symp. Quant. Biol. , vol.34 , pp. 521-528
    • Wilcox, M.1
  • 11
    • 0030613553 scopus 로고    scopus 로고
    • Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
    • Gln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation Proc. Natl. Acad. Sci. USA 94 1997 11819 11826
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11819-11826
    • Curnow, A.W.1    Hong, K.2    Yuan, R.3    Kim, S.4    Martins, O.5    Winkler, W.6
  • 12
    • 0032573080 scopus 로고    scopus 로고
    • Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
    • A.W. Curnow D.L. Tumbula J.T. Pelaschier B. Min D. Söll Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis Proc. Natl. Acad. Sci. USA 95 1998 12838 12843
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12838-12843
    • Curnow, A.W.1    Tumbula, D.L.2    Pelaschier, J.T.3    Min, B.4    Söll, D.5
  • 13
    • 0034617450 scopus 로고    scopus 로고
    • The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can also generate Gln-tRNA(Gln)
    • H.D. Becker B. Min C. Jacobi G. Raczniak J. Pelaschier H. Roy The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can also generate Gln-tRNA(Gln) FEBS Lett. 476 2000 140 144
    • (2000) FEBS Lett. , vol.476 , pp. 140-144
    • Becker, H.D.1    Min, B.2    Jacobi, C.3    Raczniak, G.4    Pelaschier, J.5    Roy, H.6
  • 14
    • 0035824544 scopus 로고    scopus 로고
    • A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis
    • G. Raczniak H.D. Becker B. Min D. Söll A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis J. Biol. Chem. 276 2001 45862 45867
    • (2001) J. Biol. Chem. , vol.276 , pp. 45862-45867
    • Raczniak, G.1    Becker, H.D.2    Min, B.3    Söll, D.4
  • 15
    • 1642459148 scopus 로고    scopus 로고
    • Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1
    • P.M. Akochy D. Bernard P.H. Roy J. Lapointe Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1 J. Bacteriol. 186 2004 767 776
    • (2004) J. Bacteriol. , vol.186 , pp. 767-776
    • Akochy, P.M.1    Bernard, D.2    Roy, P.H.3    Lapointe, J.4
  • 18
    • 33745587578 scopus 로고    scopus 로고
    • The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity
    • P. Chuawong T.L. Hendrickson The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori : anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity Biochemistry 45 2006 8079 8087
    • (2006) Biochemistry , vol.45 , pp. 8079-8087
    • Chuawong, P.1    Hendrickson, T.L.2
  • 19
    • 33845463120 scopus 로고    scopus 로고
    • A thin-layer electrophoretic assay for Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase
    • T.J. Cathopoulis P. Chuawong T.L. Hendrickson A thin-layer electrophoretic assay for Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase Anal. Biochem. 360 2007 151 153
    • (2007) Anal. Biochem. , vol.360 , pp. 151-153
    • Cathopoulis, T.J.1    Chuawong, P.2    Hendrickson, T.L.3
  • 20
    • 33745596803 scopus 로고    scopus 로고
    • Ammonia channel couples glutaminase with transamidase reactions in GatCAB
    • A. Nakamura M. Yao S. Chimnaronk N. Sakai I. Tanaka Ammonia channel couples glutaminase with transamidase reactions in GatCAB Science 312 2006 1954 1958
    • (2006) Science , vol.312 , pp. 1954-1958
    • Nakamura, A.1    Yao, M.2    Chimnaronk, S.3    Sakai, N.4    Tanaka, I.5
  • 22
    • 33745587780 scopus 로고    scopus 로고
    • Structural basis of RNA-dependent recruitment of glutamine to the genetic code
    • H. Oshikane K. Sheppard S. Fukai Y. Nakamura R. Ishitani T. Numata Structural basis of RNA-dependent recruitment of glutamine to the genetic code Science 312 2006 1950 1954
    • (2006) Science , vol.312 , pp. 1950-1954
    • Oshikane, H.1    Sheppard, K.2    Fukai, S.3    Nakamura, Y.4    Ishitani, R.5    Numata, T.6
  • 23
    • 33846203431 scopus 로고    scopus 로고
    • Co-evolution of the archaeal tRNA-dependent amidotransferase GatCAB with tRNA(Asn)
    • S. Namgoong K. Sheppard R.L. Sherrer D. Söll Co-evolution of the archaeal tRNA-dependent amidotransferase GatCAB with tRNA(Asn) FEBS Lett. 581 2007 309 314
    • (2007) FEBS Lett. , vol.581 , pp. 309-314
    • Namgoong, S.1    Sheppard, K.2    Sherrer, R.L.3    Söll, D.4
  • 25
    • 26444567797 scopus 로고    scopus 로고
    • Structural basis for tRNA-dependent amidotransferase function
    • E. Schmitt M. Panvert S. Blanquet Y. Mechulam Structural basis for tRNA-dependent amidotransferase function Structure 13 2005 1421 1433
    • (2005) Structure , vol.13 , pp. 1421-1433
    • Schmitt, E.1    Panvert, M.2    Blanquet, S.3    Mechulam, Y.4
  • 28
    • 24944555774 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of Erwinia carotovora L-asparaginase
    • G.A. Kotzia N.E. Labrou Cloning, expression and characterisation of Erwinia carotovora L-asparaginase J. Biotechnol. 119 2005 309 323
    • (2005) J. Biotechnol. , vol.119 , pp. 309-323
    • Kotzia, G.A.1    Labrou, N.E.2
  • 29
    • 0017287680 scopus 로고
    • Purification and properties of a highly potent antitumor glutaminase-asparaginase from Pseudomonas 7Z
    • J. Roberts Purification and properties of a highly potent antitumor glutaminase-asparaginase from Pseudomonas 7Z J. Biol. Chem. 251 1976 2119 2123
    • (1976) J. Biol. Chem. , vol.251 , pp. 2119-2123
    • Roberts, J.1
  • 30
    • 0023958268 scopus 로고
    • Characterization of the glutamyl-tRNA(Gln)-to-glutaminyl-tRNA(Gln) amidotransferase reaction of Bacillus subtilis
    • M.A. Strauch H. Zalkin A.I. Aronson Characterization of the glutamyl-tRNA(Gln)-to-glutaminyl-tRNA(Gln) amidotransferase reaction of Bacillus subtilis J. Bacteriol. 170 1988 916 920
    • (1988) J. Bacteriol. , vol.170 , pp. 916-920
    • Strauch, M.A.1    Zalkin, H.2    Aronson, A.I.3
  • 31
    • 0025349212 scopus 로고
    • Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii
    • D. Jahn Y.C. Kim Y. Ishino M.W. Chen D. Söll Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii J. Biol. Chem. 265 1990 8059 8064
    • (1990) J. Biol. Chem. , vol.265 , pp. 8059-8064
    • Jahn, D.1    Kim, Y.C.2    Ishino, Y.3    Chen, M.W.4    Söll, D.5
  • 32
    • 36048943978 scopus 로고    scopus 로고
    • Mechanism of a GatCAB amidotransferase: Aspartyl-tRNA synthetase increases its affinity for Asp-tRNA(Asn) and novel aminoacyl-tRNA analogues are competitive inhibitors
    • J.L. Huot C. Balg D. Jahn J. Moser A. Emond S.P. Blais Mechanism of a GatCAB amidotransferase: Aspartyl-tRNA synthetase increases its affinity for Asp-tRNA(Asn) and novel aminoacyl-tRNA analogues are competitive inhibitors Biochemistry 46 2007 13190 13198
    • (2007) Biochemistry , vol.46 , pp. 13190-13198
    • Huot, J.L.1    Balg, C.2    Jahn, D.3    Moser, J.4    Emond, A.5    Blais, S.P.6
  • 33
    • 35348989769 scopus 로고    scopus 로고
    • The transamidosome: a dynamic ribonucleoprotein particle dedicated to prokaryotic tRNA-dependent asparagine biosynthesis
    • M. Bailly M. Blaise B. Lorber H.D. Becker D. Kern The transamidosome: a dynamic ribonucleoprotein particle dedicated to prokaryotic tRNA-dependent asparagine biosynthesis Mol. Cell 28 2007 228 239
    • (2007) Mol. Cell , vol.28 , pp. 228-239
    • Bailly, M.1    Blaise, M.2    Lorber, B.3    Becker, H.D.4    Kern, D.5
  • 34
    • 0025214240 scopus 로고
    • Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins
    • M.P. Jennings I.R. Beacham Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins J. Bacteriol. 172 1990 1491 1498
    • (1990) J. Bacteriol. , vol.172 , pp. 1491-1498
    • Jennings, M.P.1    Beacham, I.R.2
  • 35
    • 0015534646 scopus 로고
    • Fine structure of Methanobacterium thermoautotrophicum: effect of growth temperature on morphology and ultrastructure
    • J.G. Zeikus R.S. Wolfe Fine structure of Methanobacterium thermoautotrophicum : effect of growth temperature on morphology and ultrastructure J. Bacteriol. 113 1973 461 467
    • (1973) J. Bacteriol. , vol.113 , pp. 461-467
    • Zeikus, J.G.1    Wolfe, R.S.2
  • 36
    • 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
    • J.C. Salazar R. Zuniga G. Raczniak H. Becker D. Söll O. Orellana 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 2001 129 131
    • (2001) FEBS Lett. , vol.500 , pp. 129-131
    • Salazar, J.C.1    Zuniga, R.2    Raczniak, G.3    Becker, H.4    Söll, D.5    Orellana, O.6
  • 37
    • 0023184331 scopus 로고
    • Bacterial evolution
    • C.R. Woese Bacterial evolution Microbiol. Rev. 51 1987 221 271
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 38
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions
    • M.D. Michelitsch J.S. Weissman A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions Proc. Natl. Acad. Sci. USA 97 2000 11910 11915
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 39
    • 0242290154 scopus 로고    scopus 로고
    • Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content
    • G.A. Singer D.A. Hickey Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content Gene 317 2003 39 47
    • (2003) Gene , vol.317 , pp. 39-47
    • Singer, G.A.1    Hickey, D.A.2
  • 40
    • 0346784967 scopus 로고
    • The determination of glutamine in the presence of asparagine
    • H.B. Vickery G.W. Pucher H.E. Clark The determination of glutamine in the presence of asparagine Biochem. J. 29 1935 2710 2720
    • (1935) Biochem. J. , vol.29 , pp. 2710-2720
    • Vickery, H.B.1    Pucher, G.W.2    Clark, H.E.3
  • 41
    • 0037020225 scopus 로고    scopus 로고
    • Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms
    • D. Tumbula-Hansen L. Feng H. Toogood K.O. Stetter D. Söll Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms J. Biol. Chem. 277 2002 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    Söll, D.5
  • 42
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 43
    • 0032566634 scopus 로고    scopus 로고
    • Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: production and activity
    • P. Fechter J. Rudinger R. Giege A. Theobald-Dietrich Ribozyme processed tRNA transcripts with unfriendly internal promoter for T7 RNA polymerase: production and activity FEBS Lett. 436 1998 99 103
    • (1998) FEBS Lett. , vol.436 , pp. 99-103
    • Fechter, P.1    Rudinger, J.2    Giege, R.3    Theobald-Dietrich, A.4
  • 44
    • 0037415690 scopus 로고    scopus 로고
    • Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae: implication for tRNA sorting mechanism
    • T. Kaneko T. Suzuki S.T. Kapushoc M.A. Rubio J. Ghazvini K. Watanabe L. Simpson Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae : implication for tRNA sorting mechanism EMBO J. 22 2003 657 667
    • (2003) EMBO J. , vol.22 , pp. 657-667
    • Kaneko, T.1    Suzuki, T.2    Kapushoc, S.T.3    Rubio, M.A.4    Ghazvini, J.5    Watanabe, K.6    Simpson, L.7


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