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Volumn 1480, Issue 1-2, 2000, Pages 160-170

Characterization of yeast seryl-tRNA synthetase active site mutants with improved discrimination against substrate analogues

Author keywords

Inhibition; Seryl tRNA synthetase; Substrate analogue

Indexed keywords

ADENOSINE DERIVATIVE; HYDROXAMIC ACID; SERINE DERIVATIVE; SERINE TRANSFER RNA LIGASE;

EID: 0342647021     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00066-2     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0031030184 scopus 로고    scopus 로고
    • Defining the active site of yeast seryl-tRNA synthetase: Mutations in motif 2 loop residues affect tRNA-dependent amino acid recognition
    • Lenhard B., Filipić S., Landeka I., Škrtić I., Söll D., Weygand-Durašević I. Defining the active site of yeast seryl-tRNA synthetase: mutations in motif 2 loop residues affect tRNA-dependent amino acid recognition. J. Biol. Chem. 272:1997;1136-1141.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1136-1141
    • Lenhard, B.1    Filipić, S.2    Landeka, I.3    Škrtić, I.4    Söll, D.5    Weygand-Durašević, I.6
  • 2
    • 0031763004 scopus 로고    scopus 로고
    • C-terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition
    • Lenhard B., Praetorius-Ibba M., Filipić S., Söll D., Weygand-Durašević I. C-terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition. FEBS Lett. 439:1998;235-240.
    • (1998) FEBS Lett. , vol.439 , pp. 235-240
    • Lenhard, B.1    Praetorius-Ibba, M.2    Filipić, S.3    Söll, D.4    Weygand-Durašević, I.5
  • 5
    • 0030011019 scopus 로고    scopus 로고
    • Ser and a seryl-adenylate analogue reveals a conformational switch in the active site
    • Ser and a seryl-adenylate analogue reveals a conformational switch in the active site. EMBO J. 15:1996;2834-2842.
    • (1996) EMBO J. , vol.15 , pp. 2834-2842
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 6
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez G.J., Moras D. Structural and functional considerations of the aminoacylation reaction. Trends Biochem. Sci. 22:1997;211-216.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 211-216
    • Arnez, G.J.1    Moras, D.2
  • 7
    • 0033198765 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: A family of expanding functions
    • Martinis S.A., Plateau P., Cavarelli J., Florentz C. Aminoacyl-tRNA synthetases: a family of expanding functions. EMBO J. 18:1999;4591-4596.
    • (1999) EMBO J. , vol.18 , pp. 4591-4596
    • Martinis, S.A.1    Plateau, P.2    Cavarelli, J.3    Florentz, C.4
  • 8
    • 0029776711 scopus 로고    scopus 로고
    • A eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryotic-like and resistant to a eubacterial-specific antysynthetase drug
    • Sassanfar M., Kranz J.E., Gallant P., Schimmel P., Shiba K. A eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryotic-like and resistant to a eubacterial-specific antysynthetase drug. Biochemistry. 35:1996;9995-10003.
    • (1996) Biochemistry , vol.35 , pp. 9995-10003
    • Sassanfar, M.1    Kranz, J.E.2    Gallant, P.3    Schimmel, P.4    Shiba, K.5
  • 10
    • 0031787909 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases as targets for new antiinfectives
    • Schimmel P., Tao J., Hill J. Aminoacyl-tRNA synthetases as targets for new antiinfectives. FASEB J. 12:1998;1599-1609.
    • (1998) FASEB J. , vol.12 , pp. 1599-1609
    • Schimmel, P.1    Tao, J.2    Hill, J.3
  • 11
    • 0033610812 scopus 로고    scopus 로고
    • Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. Mechanism of inhibition by reaction intermediate and pseudomonic acid analogues studied using transient and steady-state kinetics
    • Pope A.J., Moore K.J., McVey M., Mensah L., Benson N., Osbourne N., Broom N., Brown M.J.B., O'Hanlon P. Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. Mechanism of inhibition by reaction intermediate and pseudomonic acid analogues studied using transient and steady-state kinetics. J. Biol. Chem. 273:1998;31691-31701.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31691-31701
    • Pope, A.J.1    Moore, K.J.2    McVey, M.3    Mensah, L.4    Benson, N.5    Osbourne, N.6    Broom, N.7    Brown, M.J.B.8    O'Hanlon, P.9
  • 12
    • 0019164866 scopus 로고
    • Interaction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNA synthetase
    • Hughes J., Mellows G. Interaction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNA synthetase. Biochem. J. 191:1980;209-219.
    • (1980) Biochem. J. , vol.191 , pp. 209-219
    • Hughes, J.1    Mellows, G.2
  • 13
    • 0026095850 scopus 로고
    • Expression and characterization of a recombinant yeast isoleucyl-tRNA synthetase
    • Racher K.I., Kalmar G.B., Borgford T.J. Expression and characterization of a recombinant yeast isoleucyl-tRNA synthetase. J. Biol. Chem. 226:1991;17158-17164.
    • (1991) J. Biol. Chem. , vol.226 , pp. 17158-17164
    • Racher, K.I.1    Kalmar, G.B.2    Borgford, T.J.3
  • 14
    • 0018771039 scopus 로고
    • Interaction of indolmycin in the metabolism of tryptophan in rat liver
    • Werner R.G., Reuter W. Interaction of indolmycin in the metabolism of tryptophan in rat liver. Arzneim.Forsch. 29:1979;59-63.
    • (1979) Arzneim.Forsch. , vol.29 , pp. 59-63
    • Werner, R.G.1    Reuter, W.2
  • 17
    • 0028889651 scopus 로고
    • Update on mupirocin resistance
    • Poupard J.A. Update on mupirocin resistance. J. Chemother. 3:(suppl):1995;71-74.
    • (1995) J. Chemother. , vol.3 , Issue.SUPPL. , pp. 71-74
    • Poupard, J.A.1
  • 18
    • 0026015417 scopus 로고
    • Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations
    • Kast P., Hennecke H. Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations. J. Mol. Biol. 222:1991;99-124.
    • (1991) J. Mol. Biol. , vol.222 , pp. 99-124
    • Kast, P.1    Hennecke, H.2
  • 20
    • 0030058138 scopus 로고    scopus 로고
    • Escherichia coli tryptophanyl-tRNA synthetase mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding
    • Sever S., Rogers K., Rogers M.J., Carter C., Söll D. Escherichia coli tryptophanyl-tRNA synthetase mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding. Biochemistry. 35:1996;32-40.
    • (1996) Biochemistry , vol.35 , pp. 32-40
    • Sever, S.1    Rogers, K.2    Rogers, M.J.3    Carter, C.4    Söll, D.5
  • 21
    • 0028050510 scopus 로고
    • Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase
    • Yanagisawa T., Lee J.T., Wu H.C., Kawakami M. Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase. J. Biol. Chem. 269:1994;24304-24309.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24304-24309
    • Yanagisawa, T.1    Lee, J.T.2    Wu, H.C.3    Kawakami, M.4
  • 22
    • 0015081154 scopus 로고
    • Effect of serine hydroxamate on the growth of Escherichia coli
    • Tosa T., Pizer L.I. Effect of serine hydroxamate on the growth of Escherichia coli. J. Bacteriol. 106:1971;966-977.
    • (1971) J. Bacteriol. , vol.106 , pp. 966-977
    • Tosa, T.1    Pizer, L.I.2
  • 23
    • 0015079354 scopus 로고
    • Biochemical bases for the antimetabolite action of L-serine hydroxamate
    • Tosa T., Pizer L.I. Biochemical bases for the antimetabolite action of L-serine hydroxamate. J. Bacteriol. 106:1971;972-982.
    • (1971) J. Bacteriol. , vol.106 , pp. 972-982
    • Tosa, T.1    Pizer, L.I.2
  • 24
    • 0027155682 scopus 로고
    • Yeast seryl-tRNA synthetase expressed in E. coli recognizes bacterial serine-specific tRNAs in vivo
    • Weygand-Durašević I., Ban N., Jahn D., Söll D. Yeast seryl-tRNA synthetase expressed in E. coli recognizes bacterial serine-specific tRNAs in vivo. Eur. J. Biochem. 214:1993;869-877.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 869-877
    • Weygand-Durašević, I.1    Ban, N.2    Jahn, D.3    Söll, D.4
  • 25
    • 0030058229 scopus 로고    scopus 로고
    • The C-terminal extension of yeast seryl-tRNA synthetase affects stability of the enzyme and its substrate affinity
    • Weygand-Durašević I., Lenhard B., Filipić S., Söll D. The C-terminal extension of yeast seryl-tRNA synthetase affects stability of the enzyme and its substrate affinity. J. Biol. Chem. 271:1996;2455-2461.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2455-2461
    • Weygand-Durašević, I.1    Lenhard, B.2    Filipić, S.3    Söll, D.4
  • 26
    • 0013906160 scopus 로고
    • Purification and physical characterization of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis
    • Calendar R., Berg P. Purification and physical characterization of tyrosyl ribonucleic acid synthetases from Escherichia coli and Bacillus subtilis. Biochemistry. 5:1966;1681-1690.
    • (1966) Biochemistry , vol.5 , pp. 1681-1690
    • Calendar, R.1    Berg, P.2
  • 27
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson J.R., Uhlenbeck O.C. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. USA. 85:1988;1033-1037.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 29
    • 0025998477 scopus 로고
    • X-ray crystallographic conformational study of 5′-O-[N-(L-alanyl)-sulfamoyl]adenosine, a substrate analogue for alanyl-tRNA synthetase
    • Ueda H., Shoku Y., Hayashi N., Mitsunaga J., In Y., Doi M., Inoue M., Ishida T. X-ray crystallographic conformational study of 5′-O-[N-(L-alanyl)-sulfamoyl]adenosine, a substrate analogue for alanyl-tRNA synthetase. Biochim. Biophys. Acta. 1080:1991;126-134.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 126-134
    • Ueda, H.1    Shoku, Y.2    Hayashi, N.3    Mitsunaga, J.4    In, Y.5    Doi, M.6    Inoue, M.7    Ishida, T.8
  • 30
    • 84926319125 scopus 로고
    • Über das Hydrazidosulfamid
    • Appel R., Berger G. Über das Hydrazidosulfamid. Chem. Ber. 91:1958;1339-1341.
    • (1958) Chem. Ber. , vol.91 , pp. 1339-1341
    • Appel, R.1    Berger, G.2
  • 31
    • 0017161152 scopus 로고
    • 4′-Substituted nucleosides. 2. Synthesis of the nucleoside antibiotic nucleocitidin
    • Jenkins I.D., Verheyden J.P.H., Moffatt J.G. 4′-Substituted nucleosides. 2. Synthesis of the nucleoside antibiotic nucleocitidin. J. Am. Chem. Soc. 98:1976;3346-3357.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 3346-3357
    • Jenkins, I.D.1    Verheyden, J.P.H.2    Moffatt, J.G.3
  • 32
    • 0014939147 scopus 로고
    • Purification and properties of seryl transfer ribouncleic acid synthetase from Escherichia coli
    • Katze J.R., Konigsberg W. Purification and properties of seryl transfer ribouncleic acid synthetase from Escherichia coli. J. Biol. Chem. 245:1970;923-930.
    • (1970) J. Biol. Chem. , vol.245 , pp. 923-930
    • Katze, J.R.1    Konigsberg, W.2
  • 33
    • 0022388561 scopus 로고
    • Homotropic effects in aspartate transcarbamoylase. What happens when the enyzme binds a single molecule of the bisubstrate analog N-phosphonacetyl-aspartate?
    • Foote J., Schachman H.K. Homotropic effects in aspartate transcarbamoylase. What happens when the enyzme binds a single molecule of the bisubstrate analog N-phosphonacetyl-aspartate? J. Mol. Biol. 186:1985;175-184.
    • (1985) J. Mol. Biol. , vol.186 , pp. 175-184
    • Foote, J.1    Schachman, H.K.2
  • 35
    • 0029907152 scopus 로고    scopus 로고
    • Lys transcript anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue
    • Lys transcript anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue. EMBO J. 15:1996;6321-6334.
    • (1996) EMBO J. , vol.15 , pp. 6321-6334
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 36
    • 0031456444 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases
    • Cusack S. Aminoacyl-tRNA synthetases. Curr. Opin. Struct. Biol. 7:1997;881-889.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 881-889
    • Cusack, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.