메뉴 건너뛰기




Volumn 11, Issue 2, 1997, Pages 251-262

Cysteine synthesis in plants: Protein-protein interactions of serine acetyltransferase from Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CYSTEINE; CYSTEINE SYNTHASE; HYBRID PROTEIN; LYASE; MET17 PROTEIN, S CEREVISIAE; MULTIENZYME COMPLEX; O ACETYLHOMOSERINE (THIOL) LYASE; O-ACETYLHOMOSERINE (THIOL)-LYASE; SACCHAROMYCES CEREVISIAE PROTEIN; SERINE ACETYLTRANSFERASE;

EID: 0031079570     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1997.11020251.x     Document Type: Article
Times cited : (122)

References (56)
  • 1
    • 84941127209 scopus 로고
    • Sulfur metabolism in plants
    • Miflin, B.J. and Lea, P.J., eds. New York: Academic Press
    • Anderson, J.W. (1990) Sulfur metabolism in plants. In The Biochemistry of Plants, Volume 6 (Miflin, B.J. and Lea, P.J., eds). New York: Academic Press, pp. 327-381.
    • (1990) The Biochemistry of Plants , vol.6 , pp. 327-381
    • Anderson, J.W.1
  • 3
    • 0014670816 scopus 로고
    • Pleiotropy in a cysteine-requiring mutant of Salmonella typhimurium resulting from altered protein-protein interaction
    • Backer, M.A. and Tomkins, G.M. (1969) Pleiotropy in a cysteine-requiring mutant of Salmonella typhimurium resulting from altered protein-protein interaction. J. Biol. Chem. 244, 6023-6030.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6023-6030
    • Backer, M.A.1    Tomkins, G.M.2
  • 4
    • 0028938619 scopus 로고
    • Cysteine biosynthesis in plants: Isolation and functional characterization of a cDNA encoding serine acetyltransferase from Arabidopsis thaliana
    • Bogdanova, N., Bork, C. and Hell, R. (1995) Cysteine biosynthesis in plants: isolation and functional characterization of a cDNA encoding serine acetyltransferase from Arabidopsis thaliana. FEBS Lett. 358, 43-47.
    • (1995) FEBS Lett. , vol.358 , pp. 43-47
    • Bogdanova, N.1    Bork, C.2    Hell, R.3
  • 5
    • 0025047458 scopus 로고
    • Glutamyl-tRNA synthetase of Bacillus subtilis 168T and of Bacillus stearothermophilus
    • Breton, R., Watson, D., Vaguchi, M. and Lapointe, J. (1990) Glutamyl-tRNA synthetase of Bacillus subtilis 168T and of Bacillus stearothermophilus. J. Biol. Chem. 265, 18 248-18 255.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18248-18255
    • Breton, R.1    Watson, D.2    Vaguchi, M.3    Lapointe, J.4
  • 6
    • 0001982503 scopus 로고
    • Regulatory interaction between sulfate and nitrogen metabolism
    • De Kok, L.J., Stulen, I., Rennenberg, H., Brunold, C. and Rauser, W.E., eds. The Hague: SPB Academic Publishers
    • Brunold, C. (1993) Regulatory interaction between sulfate and nitrogen metabolism. In Sulfur Nutrition and Assimilation in Higher Plants (De Kok, L.J., Stulen, I., Rennenberg, H., Brunold, C. and Rauser, W.E., eds). The Hague: SPB Academic Publishers, pp. 61-76.
    • (1993) Sulfur Nutrition and Assimilation in Higher Plants , pp. 61-76
    • Brunold, C.1
  • 7
    • 0000485535 scopus 로고
    • Intracellular localization of serine acetyltransferase in spinach leaves
    • Brunold, C. and Suter, M. (1982) Intracellular localization of serine acetyltransferase in spinach leaves. Planta, 155, 321-327.
    • (1982) Planta , vol.155 , pp. 321-327
    • Brunold, C.1    Suter, M.2
  • 8
    • 0026598896 scopus 로고
    • Genetic analysis of a new mutation conferring cysteine auxotrophy in Saccharomyces cerevisiae: Updating of the sulfur metabolism pathway
    • Cherest, H. and Surdin-Kerjan, Y. (1992) Genetic analysis of a new mutation conferring cysteine auxotrophy in Saccharomyces cerevisiae: updating of the sulfur metabolism pathway. Genetics, 130, 51-58.
    • (1992) Genetics , vol.130 , pp. 51-58
    • Cherest, H.1    Surdin-Kerjan, Y.2
  • 9
    • 0026639625 scopus 로고
    • Protein interaction cloning in yeast: Identification of mammalian proteins that react with the leucine zipper of Jun
    • Chevray, P.M. and Nathans, D. (1992) Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc. Natl Acad. Sci. USA, 89, 5789-5793.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5789-5793
    • Chevray, P.M.1    Nathans, D.2
  • 10
    • 0017594294 scopus 로고
    • Initial kinetic characterization of the multienzyme complex, cysteine synthetase
    • Cook, P.F. and Wedding, R.T. (1977) Initial kinetic characterization of the multienzyme complex, cysteine synthetase. Arch. Biochem. Biophys. 178, 293-302.
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 293-302
    • Cook, P.F.1    Wedding, R.T.2
  • 11
    • 0023097071 scopus 로고
    • L-Cysteine biosynthesis in Escherichia coli: Nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant
    • Denk, D. and Böck, A. (1987) L-Cysteine biosynthesis in Escherichia coli: nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant. J. Gen. Microbiol. 133, 515-525.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 515-525
    • Denk, D.1    Böck, A.2
  • 12
    • 0026544820 scopus 로고
    • What is known about the structure and function of the Escherichia coli protein FirA?
    • Dicker, I.B. and Seethraram, S. (1992) What is known about the structure and function of the Escherichia coli protein FirA? Mol. Microbiol. 6, 817-823.
    • (1992) Mol. Microbiol. , vol.6 , pp. 817-823
    • Dicker, I.B.1    Seethraram, S.2
  • 13
    • 0026637901 scopus 로고
    • Purification and characterization of O-acetylserine (thiol) lyase from spinach chloroplasts
    • Droux, M., Martin, J., Sajus, P. and Douce, R. (1992) Purification and characterization of O-acetylserine (thiol) lyase from spinach chloroplasts. Arch. Biochem. Biophys. 295, 379-390.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 379-390
    • Droux, M.1    Martin, J.2    Sajus, P.3    Douce, R.4
  • 14
    • 0026044974 scopus 로고
    • Nucleotide sequence and genetic analysis of the Azotobacter chroococcum nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine acetyltransferase
    • Evans, D.J., Jones, R., Woodley, P.R., Wilborn, J.R. and Robson, R.L (1991) Nucleotide sequence and genetic analysis of the Azotobacter chroococcum nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine acetyltransferase. J. Bacteriol. 173, 5457-5469.
    • (1991) J. Bacteriol. , vol.173 , pp. 5457-5469
    • Evans, D.J.1    Jones, R.2    Woodley, P.R.3    Wilborn, J.R.4    Robson, R.L.5
  • 15
    • 0028263738 scopus 로고
    • Construction of an improved host strain for two hybrid screening
    • Feilotter, H.E., Hannon, G.J., Ruddel, C.J. and Beach, D. (1994) Construction of an improved host strain for two hybrid screening. Nucl. Acids Res. 22, 1502-1503.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1502-1503
    • Feilotter, H.E.1    Hannon, G.J.2    Ruddel, C.J.3    Beach, D.4
  • 16
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. and Song, O. (1989) A novel genetic system to detect protein-protein interactions. Nature, 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 17
    • 0028124463 scopus 로고
    • The two-hybrid-system: Assay for protein-protein interactions
    • Fields, S. and Sternglanz, R. (1994) The two-hybrid-system: assay for protein-protein interactions. Trends Genet. 10, 286-291.
    • (1994) Trends Genet. , vol.10 , pp. 286-291
    • Fields, S.1    Sternglanz, R.2
  • 18
    • 0001939094 scopus 로고
    • RACE: Rapid amplification of cDNA ends
    • Innis, M.A., Gelfand, D.H., Sninsky, J.J. and White, T.J., eds. San Diego: Academic Press
    • Frohman, M.A. (1990) RACE: rapid amplification of cDNA ends. In PCR Protocols. A Guide to Methods and Applications (Innis, M.A., Gelfand, D.H., Sninsky, J.J. and White, T.J., eds). San Diego: Academic Press, pp. 28-38.
    • (1990) PCR Protocols. a Guide to Methods and Applications , pp. 28-38
    • Frohman, M.A.1
  • 20
    • 0026097503 scopus 로고
    • Chloroplast transit peptides. the perfect random coil?
    • von Heijne, G. and Nishikawa, K. (1991) Chloroplast transit peptides. The perfect random coil? FEBS Lett. 278, 1-3.
    • (1991) FEBS Lett. , vol.278 , pp. 1-3
    • Von Heijne, G.1    Nishikawa, K.2
  • 21
    • 0000036169 scopus 로고
    • Characterization of a full-length cDNA encoding serine acetyltransferase from Arabidopsis thaliana [X80938] (PGR95-108)
    • Hell, R. and Bogdanova, N. (1995) Characterization of a full-length cDNA encoding serine acetyltransferase from Arabidopsis thaliana [X80938] (PGR95-108). Plant Physiol. 109, 1498.
    • (1995) Plant Physiol. , vol.109 , pp. 1498
    • Hell, R.1    Bogdanova, N.2
  • 22
    • 0028025227 scopus 로고
    • Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana
    • Hell, R., Bork, C., Bogdanova, N., Frolov, I. and Hauschild, R. (1994) Isolation and characterization of two cDNAs encoding for compartment specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis thaliana. FEBS Lett. 351, 257-262.
    • (1994) FEBS Lett. , vol.351 , pp. 257-262
    • Hell, R.1    Bork, C.2    Bogdanova, N.3    Frolov, I.4    Hauschild, R.5
  • 23
    • 0001575175 scopus 로고
    • Purification and characterization of cysteine syntheses from Citrullus vulgaris
    • Ikegami, F., Kaneko, M., Kamiyama, H. and Murakoshi, I. (1988) Purification and characterization of cysteine syntheses from Citrullus vulgaris. Phytochemistry, 27, 697-701.
    • (1988) Phytochemistry , vol.27 , pp. 697-701
    • Ikegami, F.1    Kaneko, M.2    Kamiyama, H.3    Murakoshi, I.4
  • 24
    • 44049111777 scopus 로고
    • Purification and characterization of two forms of cysteine synthase from Allium tuberosum
    • Ikegami, F., Itagaki, S. and Murakoshi, I. (1993) Purification and characterization of two forms of cysteine synthase from Allium tuberosum. Phytochemistry, 32, 31-34.
    • (1993) Phytochemistry , vol.32 , pp. 31-34
    • Ikegami, F.1    Itagaki, S.2    Murakoshi, I.3
  • 25
    • 0023056199 scopus 로고
    • Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene
    • Kerjan, P., Cherest, H. and Surdin-Kerjan, Y. (1986) Nucleotide sequence of the Saccharomyces cerevisiae MET25 gene. Nucl. Acids Res. 14, 7861-7871.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 7861-7871
    • Kerjan, P.1    Cherest, H.2    Surdin-Kerjan, Y.3
  • 27
    • 0014011576 scopus 로고
    • The enzymatic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium
    • Kredich, N.M. and Tomkins, G.M. (1966) The enzymatic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J. Biol. Chem. 241, 4955-4965.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4955-4965
    • Kredich, N.M.1    Tomkins, G.M.2
  • 28
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • Kredich, N.M., Becker, M.A. and Tomkins, G.M. (1969) Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. J. Biol. Chem. 244, 2428-2439.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 30
    • 0026649124 scopus 로고
    • Sequence analysis of a DNA fragment from Buchnera aphidicola (an endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE, and secB
    • Lai, C.-Y. and Baumann, P. (1992) Sequence analysis of a DNA fragment from Buchnera aphidicola (an endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE, and secB. Gene, 119, 113-118.
    • (1992) Gene , vol.119 , pp. 113-118
    • Lai, C.-Y.1    Baumann, P.2
  • 31
    • 0022895249 scopus 로고
    • The MET2 gene of Saccharomyces cerevisiae: Molecular cloning and nucleotide sequence
    • Langin, T., Faugeron, G., Goyon, C., Nicolas, A. and Rossignol, J.-L. (1986) The MET2 gene of Saccharomyces cerevisiae: Molecular cloning and nucleotide sequence. Gene, 49, 283-293.
    • (1986) Gene , vol.49 , pp. 283-293
    • Langin, T.1    Faugeron, G.2    Goyon, C.3    Nicolas, A.4    Rossignol, J.-L.5
  • 32
    • 0001113803 scopus 로고
    • Localization of ATP-sulfurylase and O-acetylserine(thiol)lyase in spinach leaves
    • Lunn, J.E., Droux, M., Martin, J. and Douce, R. (1990) Localization of ATP-sulfurylase and O-acetylserine(thiol)lyase in spinach leaves. Plant Physiol. 94, 1345-1352.
    • (1990) Plant Physiol. , vol.94 , pp. 1345-1352
    • Lunn, J.E.1    Droux, M.2    Martin, J.3    Douce, R.4
  • 33
    • 0029421132 scopus 로고
    • Serine acetyltransferase from Arabidopsis thaliana can functionally complement the cysteine requirement of a cysE mutant strain of Escherichia coli
    • Murillo, M., Foglia, R., Diller, A., Lee, S. and Leustek, T. (1995) Serine acetyltransferase from Arabidopsis thaliana can functionally complement the cysteine requirement of a cysE mutant strain of Escherichia coli. Cell. Mol. Biol. 41, 425-433.
    • (1995) Cell. Mol. Biol. , vol.41 , pp. 425-433
    • Murillo, M.1    Foglia, R.2    Diller, A.3    Lee, S.4    Leustek, T.5
  • 34
    • 0001398281 scopus 로고
    • Isolation of serine acetyltransferase complexed with cysteine synthase from Allium tuberosum
    • Nakamura, K. and Tamura, G. (1990) Isolation of serine acetyltransferase complexed with cysteine synthase from Allium tuberosum. J. Biol. Chem. 54, 649-656.
    • (1990) J. Biol. Chem. , vol.54 , pp. 649-656
    • Nakamura, K.1    Tamura, G.2
  • 35
    • 0000760333 scopus 로고
    • Measurement of serine acetyltransferase activity in crude plant extracts by a coupled assay system using cysteine synthase
    • Nakamura, K., Hayama, A., Masada, M., Fukushima, K. and Tamura, G. (1987) Measurement of serine acetyltransferase activity in crude plant extracts by a coupled assay system using cysteine synthase. Plant Cell Physiol. 28, 885-891.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 885-891
    • Nakamura, K.1    Hayama, A.2    Masada, M.3    Fukushima, K.4    Tamura, G.5
  • 36
    • 0001552684 scopus 로고
    • Regulation of sulfate assimilation by light and O-acetylserine in Lemna minor L
    • Neuenschwander, U., Suter, M. and Brunold, C. (1991) Regulation of sulfate assimilation by light and O-acetylserine in Lemna minor L. Plant Physiol. 97, 253-258.
    • (1991) Plant Physiol. , vol.97 , pp. 253-258
    • Neuenschwander, U.1    Suter, M.2    Brunold, C.3
  • 37
    • 0028674857 scopus 로고
    • Genes galore: A summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones
    • Newman, T., de Bruijn, F. J., Green, P. et al. (1994) Genes galore: a summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones. Plant Physiol. 106, 1241-1255.
    • (1994) Plant Physiol. , vol.106 , pp. 1241-1255
    • Newman, T.1    De Bruijn, F.J.2    Green, P.3
  • 38
    • 0000011327 scopus 로고
    • Chloroplast cysteine synthases of Trifolium repens and Pisum sativum
    • Ng, B.H. and Andersen, J.W. (1978) Chloroplast cysteine synthases of Trifolium repens and Pisum sativum. Phytochemistry, 17, 879-885.
    • (1978) Phytochemistry , vol.17 , pp. 879-885
    • Ng, B.H.1    Andersen, J.W.2
  • 39
    • 0016194655 scopus 로고
    • The enzymatic synthesis of L-cysteine in higher plants
    • Ngo, T.T. and Shargool, P.D. (1974) The enzymatic synthesis of L-cysteine in higher plants. Can. J. Biochem. 52, 435-440.
    • (1974) Can. J. Biochem. , vol.52 , pp. 435-440
    • Ngo, T.T.1    Shargool, P.D.2
  • 40
    • 0028997929 scopus 로고
    • Two enzymes together capable of cysteine biosynthesis are encoded on a cyanobacterial plasmid
    • Nicholson, M.L., Gaasenbeek, M. and Laudenbach, D.E. (1995) Two enzymes together capable of cysteine biosynthesis are encoded on a cyanobacterial plasmid. Mol. Gen. Genet. 247, 623-632.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 623-632
    • Nicholson, M.L.1    Gaasenbeek, M.2    Laudenbach, D.E.3
  • 41
    • 0026629027 scopus 로고
    • The chloramphenicol acetyltransferase gene of Tn2424: A new breed of cat
    • Parent, R. and Roy, P.M. (1992) The chloramphenicol acetyltransferase gene of Tn2424: a new breed of cat. J. Bacteriol. 174, 2891-2897.
    • (1992) J. Bacteriol. , vol.174 , pp. 2891-2897
    • Parent, R.1    Roy, P.M.2
  • 42
    • 0001050513 scopus 로고
    • Role of O-acetylserine in hydrogen sulfide emission from pumpkin leaves in response to sulfate
    • Rennenberg, H. (1983) Role of O-acetylserine in hydrogen sulfide emission from pumpkin leaves in response to sulfate. Plant Physiol. 73, 560-565.
    • (1983) Plant Physiol. , vol.73 , pp. 560-565
    • Rennenberg, H.1
  • 43
    • 0000153222 scopus 로고
    • Subcellular distribution of O-acetylserine(thiol)lyase in cauliflower (Brassica oleracea L.) inflorescens
    • Rolland, N., Droux, M. and Douce, R. (1992) Subcellular distribution of O-acetylserine(thiol)lyase in cauliflower (Brassica oleracea L.) inflorescens. Plant Physiol. 98, 927-935.
    • (1992) Plant Physiol. , vol.98 , pp. 927-935
    • Rolland, N.1    Droux, M.2    Douce, R.3
  • 44
    • 0028065645 scopus 로고
    • Purification and kinetic properties of serine acetyltransferase free of O-acetylserine(thiol)lyase from spinach chloroplasts
    • Ruffet, M.-L., Droux, M. and Douce, R. (1994) Purification and kinetic properties of serine acetyltransferase free of O-acetylserine(thiol)lyase from spinach chloroplasts. Plant Physiol. 104, 597-604.
    • (1994) Plant Physiol. , vol.104 , pp. 597-604
    • Ruffet, M.-L.1    Droux, M.2    Douce, R.3
  • 45
    • 0028893483 scopus 로고
    • Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform
    • Ruffet, M.-L., Lebrun, M., Droux, M. and Douce, R. (1995) Subcellular distribution of serine acetyltransferase from Pisum sativum and characterization of an Arabidopsis thaliana putative cytosolic isoform. Eur. J. Biochem. 227, 500-509.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 500-509
    • Ruffet, M.-L.1    Lebrun, M.2    Droux, M.3    Douce, R.4
  • 46
    • 0028534746 scopus 로고
    • Modulation of cysteine biosynthesis in chloroplasts of transgenic tobacco overexpressing cysteine synthase (O-acetylserine(thiol)-lyase)
    • Saito, K., Kurosawa, M., Tatsuguchi, K., Tagaki, Y. and Murakoshi, I. (1994) Modulation of cysteine biosynthesis in chloroplasts of transgenic tobacco overexpressing cysteine synthase (O-acetylserine(thiol)-lyase). Plant Physiol. 106, 887-895
    • (1994) Plant Physiol. , vol.106 , pp. 887-895
    • Saito, K.1    Kurosawa, M.2    Tatsuguchi, K.3    Tagaki, Y.4    Murakoshi, I.5
  • 47
    • 0029028281 scopus 로고
    • Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon
    • Saito, K., Yokoyama, H., Noji, M. and Murakoshi, I. (1995) Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon. J. Biol. Chem. 270, 16321-16326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16321-16326
    • Saito, K.1    Yokoyama, H.2    Noji, M.3    Murakoshi, I.4
  • 49
    • 0002326857 scopus 로고
    • Sulphur metabolism D. Cysteine synthase
    • Dey, P.M. and Harborne, J.B., eds. London: Academic Press
    • Schmidt, A. (1990) Sulphur metabolism D. Cysteine synthase. In Methods in Plant Biochemistry, Volume 3 (Dey, P.M. and Harborne, J.B., eds). London: Academic Press, pp. 349-354.
    • (1990) Methods in Plant Biochemistry , vol.3 , pp. 349-354
    • Schmidt, A.1
  • 51
    • 0015217099 scopus 로고
    • Purification and characterization of L-serine transacetylase and O-acetylserine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris)
    • Smith, I.K. (1971) Purification and characterization of L-serine transacetylase and O-acetylserine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris). Biochim. Biophys. Acta, 277, 288-295.
    • (1971) Biochim. Biophys. Acta , vol.277 , pp. 288-295
    • Smith, I.K.1
  • 52
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P.A. (1987) Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56, 89-124.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 53
    • 0025978954 scopus 로고
    • Nucleotide sequence analysis of a chloramphenicol-resistance determinant from Agrobacterium tumefaciens and identification of its gene product
    • Tennigkeit, J. and Matzura, H. (1991) Nucleotide sequence analysis of a chloramphenicol-resistance determinant from Agrobacterium tumefaciens and identification of its gene product. Gene, 98, 113-116.
    • (1991) Gene , vol.98 , pp. 113-116
    • Tennigkeit, J.1    Matzura, H.2
  • 54
    • 0027121143 scopus 로고
    • Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme
    • Vaara, M. (1992) Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme. FEMS Microbiol. Lett. 97, 249-254.
    • (1992) FEMS Microbiol. Lett. , vol.97 , pp. 249-254
    • Vaara, M.1
  • 55
    • 0028031940 scopus 로고
    • The novel hexapeptide motif found in the acyltransferase IpxA and IpxD of lipid A biosynthesis is conserved in various bacteria
    • Vuorio, R., Harkonen, T., Tolvanen, M. and Vaara, M. (1994) The novel hexapeptide motif found in the acyltransferase IpxA and IpxD of lipid A biosynthesis is conserved in various bacteria. FEBS Lett. 292, 90-94.
    • (1994) FEBS Lett. , vol.292 , pp. 90-94
    • Vuorio, R.1    Harkonen, T.2    Tolvanen, M.3    Vaara, M.4
  • 56
    • 0025647853 scopus 로고
    • The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis
    • Wigley, D.B., Derrick, J.P. and Shaw, W.V. (1990) The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis. Febs Lett. 277, 267-271.
    • (1990) Febs Lett. , vol.277 , pp. 267-271
    • Wigley, D.B.1    Derrick, J.P.2    Shaw, W.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.