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Volumn 72, Issue 7, 2006, Pages 4735-4742

Effect of drug transporter genes on cysteine export and overproduction in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DRUG THERAPY; ENZYME INHIBITION; GENETIC ENGINEERING; GLUCOSE; PROTEINS;

EID: 33746060524     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02507-05     Document Type: Article
Times cited : (60)

References (39)
  • 1
    • 0041661883 scopus 로고    scopus 로고
    • Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli
    • Awano, N., M. Wada, A. Kohdoh, T. Oikawa, H. Takagi, and S. Nakamori. 2003. Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli. Appl. Microbiol. Biotechnol. 62:239-243.
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 239-243
    • Awano, N.1    Wada, M.2    Kohdoh, A.3    Oikawa, T.4    Takagi, H.5    Nakamori, S.6
  • 2
    • 22144456756 scopus 로고    scopus 로고
    • Identification and functional analysis of cysteine desulfhydrases in Escherichia coli
    • Awano, N., M. Wada, H. Mori, S. Nakamori, and H. Takagi. 2005. Identification and functional analysis of cysteine desulfhydrases in Escherichia coli. Appl. Environ. Microbiol. 71:4149-4152.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4149-4152
    • Awano, N.1    Wada, M.2    Mori, H.3    Nakamori, S.4    Takagi, H.5
  • 3
    • 0027324803 scopus 로고
    • Cloning and sequence analysis of an Escherichia coli gene conferring bicyclomycin resistance
    • Bentley, J., L. S. Hyatt, K. Ainley, J. H. Parish, R. B. Herbert, and G. R. White. 1993. Cloning and sequence analysis of an Escherichia coli gene conferring bicyclomycin resistance. Gene 127:117-120.
    • (1993) Gene , vol.127 , pp. 117-120
    • Bentley, J.1    Hyatt, L.S.2    Ainley, K.3    Parish, J.H.4    Herbert, R.B.5    White, G.R.6
  • 5
    • 0033968656 scopus 로고    scopus 로고
    • Oxidase and periplasmic cytochrome assembly in Escherichia coli K-12: CydDC and CcmAB are not required for haem-membrane association
    • Cook, G. M., and R. K. Poole. 2000. Oxidase and periplasmic cytochrome assembly in Escherichia coli K-12: CydDC and CcmAB are not required for haem-membrane association. Microbiology 146:527-536.
    • (2000) Microbiology , vol.146 , pp. 527-536
    • Cook, G.M.1    Poole, R.K.2
  • 6
    • 0012151584 scopus 로고    scopus 로고
    • Identification of a major facilitator protein from Escherichia coli involved in efflux of metabolites of the cysteine pathway
    • Daßler, T., T. Maier, C. Winterhalter, and A. Böck. 2000. Identification of a major facilitator protein from Escherichia coli involved in efflux of metabolites of the cysteine pathway. Mol. Microbiol. 36:1101-1112.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1101-1112
    • Daßler, T.1    Maier, T.2    Winterhalter, C.3    Böck, A.4
  • 8
    • 0026531624 scopus 로고
    • Isolation and characterization of the Escherichia coli htrD gene, whose product is required for growth at high temperatures
    • Delaney, J. M., D. Ang, and C. Georgopoulos. 1992. Isolation and characterization of the Escherichia coli htrD gene, whose product is required for growth at high temperatures. J. Bacteriol. 174:1240-1247.
    • (1992) J. Bacteriol. , vol.174 , pp. 1240-1247
    • Delaney, J.M.1    Ang, D.2    Georgopoulos, C.3
  • 9
    • 0023097071 scopus 로고
    • L-Cysteine biosynthesis in Escherichia coli: Nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and cysteine excreting mutant
    • Denk, D., and A. Böck. 1987. L-Cysteine biosynthesis in Escherichia coli: nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and cysteine excreting mutant. J. Gen. Microbiol. 133:515-525.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 515-525
    • Denk, D.1    Böck, A.2
  • 10
    • 0020317656 scopus 로고
    • Cloning, purification, and characterization of β-cystathionase from Escherichia coli
    • Dwivedi, C. M., R. C. Ragin, and J. R. Uren. 1982. Cloning, purification, and characterization of β-cystathionase from Escherichia coli. Biochemistry 21:3064-3069.
    • (1982) Biochemistry , vol.21 , pp. 3064-3069
    • Dwivedi, C.M.1    Ragin, R.C.2    Uren, J.R.3
  • 11
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., E. Schwarz, M. Komaromy, and R. Wall. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 12
    • 0037312795 scopus 로고    scopus 로고
    • YfiK from Escherichia coli promotes export of O-acetylserine and cysteine
    • Franke, I., A. Resch, T. Daßler, T. Maier, and A. Böck. 2003. YfiK from Escherichia coli promotes export of O-acetylserine and cysteine. J. Bacteriol. 185:1161-1166.
    • (2003) J. Bacteriol. , vol.185 , pp. 1161-1166
    • Franke, I.1    Resch, A.2    Daßler, T.3    Maier, T.4    Böck, A.5
  • 13
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde, M. K. 1967. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem. J. 104:627-633.
    • (1967) Biochem. J. , vol.104 , pp. 627-633
    • Gaitonde, M.K.1
  • 14
    • 0035101356 scopus 로고    scopus 로고
    • Genes involved in copper homeostasis in Escherichia coli
    • Grass, G., and C. Rensing. 2001. Genes involved in copper homeostasis in Escherichia coli. J. Bacteriol. 183:2145-2147.
    • (2001) J. Bacteriol. , vol.183 , pp. 2145-2147
    • Grass, G.1    Rensing, C.2
  • 15
    • 0019496855 scopus 로고
    • Cysteine and growth inhibition of Escherichia coli: Threonine deaminase as the target enzyme
    • Harris, C. L. 1981. Cysteine and growth inhibition of Escherichia coli: threonine deaminase as the target enzyme. J. Bacteriol. 145:1031-1035.
    • (1981) J. Bacteriol. , vol.145 , pp. 1031-1035
    • Harris, C.L.1
  • 16
    • 0019808826 scopus 로고
    • Cysteine and growth inhibition of Escherichia coli: Depression of the ilvGEDA operon
    • Harris, C. L., and L. Lui. 1981. Cysteine and growth inhibition of Escherichia coli: depression of the ilvGEDA operon. Biochem. Biophys. Res. Commun. 101:1145-1151.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 1145-1151
    • Harris, C.L.1    Lui, L.2
  • 17
    • 0015151856 scopus 로고
    • Mechanism of the growth inhibitory effect of cysteine on Escherichia coli
    • Kari, C., Z. Nagy, P. Kovacs, and F. Hernadi. 1971. Mechanism of the growth inhibitory effect of cysteine on Escherichia coli. J. Gen. Microbiol. 68:349-356.
    • (1971) J. Gen. Microbiol. , vol.68 , pp. 349-356
    • Kari, C.1    Nagy, Z.2    Kovacs, P.3    Hernadi, F.4
  • 19
    • 0013121536 scopus 로고
    • Regulation of cysteine biosynthesis in Escherichia coli and Salmonella typhimurium
    • K. M. Herrmann and R. L. Sommerville (ed.). Addison-Wesley Publishing Company, London, United Kingdom
    • Kredich, N. M. 1983. Regulation of cysteine biosynthesis in Escherichia coli and Salmonella typhimurium, p. 115-132. In K. M. Herrmann and R. L. Sommerville (ed.), Amino acids: biosynthesis and genetic regulation. Addison-Wesley Publishing Company, London, United Kingdom.
    • (1983) Amino Acids: Biosynthesis and Genetic Regulation , pp. 115-132
    • Kredich, N.M.1
  • 20
    • 0026686805 scopus 로고
    • Emr, an Escherichia coli locus for multidrug resistance
    • Lomovskaya, O., and K. Lewis. 1992. Emr, an Escherichia coli locus for multidrug resistance. Proc. Natl. Acad. Sci. USA 89:8938-8942.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8938-8942
    • Lomovskaya, O.1    Lewis, K.2
  • 21
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 22
    • 0031834075 scopus 로고    scopus 로고
    • Overproduction of L-cysteine and L-cystine by Escherichia coli strains with a genetically altered serine acetyltransferase
    • Nakamori, S., S. Kobayashi, C. Kobayashi, and H. Takagi. 1998. Overproduction of L-cysteine and L-cystine by Escherichia coli strains with a genetically altered serine acetyltransferase. Appl. Environ. Microbiol. 64:1607-1611.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1607-1611
    • Nakamori, S.1    Kobayashi, S.2    Kobayashi, C.3    Takagi, H.4
  • 23
    • 0000907566 scopus 로고
    • Catalytic properties of tryptophanase, a multifunctional pyridoxal phosphate enzyme
    • Newton, W. A., and E. F. Snell. 1964. Catalytic properties of tryptophanase, a multifunctional pyridoxal phosphate enzyme. Proc. Natl. Acad. Sci. USA 51:382-389.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 382-389
    • Newton, W.A.1    Snell, E.F.2
  • 24
    • 0000489511 scopus 로고
    • Properties of crystalline tryptophanase
    • Newton, W. A., Y. Morino, and E. F. Snell. 1965. Properties of crystalline tryptophanase. J. Biol. Chem. 240:1211-1218.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1211-1218
    • Newton, W.A.1    Morino, Y.2    Snell, E.F.3
  • 25
    • 0034817367 scopus 로고    scopus 로고
    • Analysis of a complete library of putative drug transporter genes in Escherichia coli
    • Nishino, K., and A. Yamaguchi. 2001. Analysis of a complete library of putative drug transporter genes in Escherichia coli. J. Bacteriol. 183:5803-5812.
    • (2001) J. Bacteriol. , vol.183 , pp. 5803-5812
    • Nishino, K.1    Yamaguchi, A.2
  • 26
    • 0037336269 scopus 로고    scopus 로고
    • High levels of intracellular cysteine promote oxidative DNA damage by driving the Fenton reaction
    • Park, S., and J. A. Imlay. 2003. High levels of intracellular cysteine promote oxidative DNA damage by driving the Fenton reaction. J. Bacteriol. 185:1942-1950.
    • (2003) J. Bacteriol. , vol.185 , pp. 1942-1950
    • Park, S.1    Imlay, J.A.2
  • 27
    • 0037147266 scopus 로고    scopus 로고
    • Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly
    • Pittman, M. S., H. Corker, G. Wu, M. B. Binet, A. J. G. Moir, and R. K. Poole. 2002. Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly. J. Biol. Chem. 277:49841-49849.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49841-49849
    • Pittman, M.S.1    Corker, H.2    Wu, G.3    Binet, M.B.4    Moir, A.J.G.5    Poole, R.K.6
  • 29
    • 0034090541 scopus 로고    scopus 로고
    • AcrD of Escherichia coli is an aminoglycoside efflux pump
    • Rosenberg, E. Y., D. Ma, and H. Nikaido. 2000. AcrD of Escherichia coli is an aminoglycoside efflux pump. J. Bacteriol. 182:1754-1756.
    • (2000) J. Bacteriol. , vol.182 , pp. 1754-1756
    • Rosenberg, E.Y.1    Ma, D.2    Nikaido, H.3
  • 32
    • 0023066723 scopus 로고
    • Microbial sulfur amino acids: An overview
    • Soda, K. 1987. Microbial sulfur amino acids: an overview. Methods Enzymol. 143:453-459.
    • (1987) Methods Enzymol. , vol.143 , pp. 453-459
    • Soda, K.1
  • 33
    • 0026332292 scopus 로고
    • Cysteine, even in low concentrations, induces transient amino acid starvation in Escherichia coli
    • Sorensen, M. A., and S. Pedersen. 1991. Cysteine, even in low concentrations, induces transient amino acid starvation in Escherichia coli. J. Bacteriol. 173:5244-5246.
    • (1991) J. Bacteriol. , vol.173 , pp. 5244-5246
    • Sorensen, M.A.1    Pedersen, S.2
  • 34
    • 0033004153 scopus 로고    scopus 로고
    • PCR random mutagenesis into Escherichia coli serine acetyltransferase: Isolation of the mutant enzymes that cause overproduction of L-cysteine and L-cystine due to the desensitization to feedback inhibition
    • Takagi, H., C. Kobayashi, S. Kobayashi, and S. Nakamori. 1999. PCR random mutagenesis into Escherichia coli serine acetyltransferase: isolation of the mutant enzymes that cause overproduction of L-cysteine and L-cystine due to the desensitization to feedback inhibition. FEBS Lett. 452:323-327.
    • (1999) FEBS Lett. , vol.452 , pp. 323-327
    • Takagi, H.1    Kobayashi, C.2    Kobayashi, S.3    Nakamori, S.4
  • 35
    • 0032846441 scopus 로고    scopus 로고
    • Overproduction of L-cysteine and L-cystine by expression of genes for feedback inhibition-insensitive serine acetyltransferase from Arabidopsis thaliana in Escherichia coli
    • Takagi, H., N. Awano, S. Kobayashi, C. Kobayashi, M. Noji, K. Saito, and S. Nakamori. 1999. Overproduction of L-cysteine and L-cystine by expression of genes for feedback inhibition-insensitive serine acetyltransferase from Arabidopsis thaliana in Escherichia coli. FEMS Microbiol. Lett. 179:453-459.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 453-459
    • Takagi, H.1    Awano, N.2    Kobayashi, S.3    Kobayashi, C.4    Noji, M.5    Saito, K.6    Nakamori, S.7
  • 36
    • 0001846893 scopus 로고
    • On the bioassay of amino acids. II. Determination of arginine, aspartic acid and cysteine
    • Tsunoda, T., S. Eguchi, and K. Narumi. 1961. On the bioassay of amino acids. II. Determination of arginine, aspartic acid and cysteine. Amino Acids 3:7-13.
    • (1961) Amino Acids , vol.3 , pp. 7-13
    • Tsunoda, T.1    Eguchi, S.2    Narumi, K.3
  • 38
    • 0029017451 scopus 로고
    • Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli
    • Wrzesinski, J., A. Bakin, K. Nurse, B. G. Lane, and J. Ofengand. 1995. Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli. Biochemistry 34:8904-8913.
    • (1995) Biochemistry , vol.34 , pp. 8904-8913
    • Wrzesinski, J.1    Bakin, A.2    Nurse, K.3    Lane, B.G.4    Ofengand, J.5
  • 39
    • 0027460297 scopus 로고
    • + antiporter of Escherichia coli encoded by transposon Tn10. The structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9
    • + antiporter of Escherichia coli encoded by transposon Tn10. The structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9. J. Biol. Chem. 268:6496-6504.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6496-6504
    • Yamaguchi, A.1    Kimura, T.2    Someya, Y.3    Sawai, T.4


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