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Volumn 649, Issue 1-2, 2008, Pages 239-244

Characterization of mutations induced by N-methyl-N′-nitro-N-nitrosoguanidine in an industrial Corynebacterium glutamicum strain

Author keywords

Corynebacterium glutamicum; Mutagenic specificity; N Methyl N nitro N nitrosoguanidine; Strain improvement

Indexed keywords

AMINO ACID; GLUCOSE; LYSINE; METHYLNITRONITROSOGUANIDINE;

EID: 36849086397     PISSN: 13835718     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrgentox.2007.10.003     Document Type: Article
Times cited : (36)

References (30)
  • 1
    • 0003051933 scopus 로고
    • Glutamic acid bacteria
    • Demain A.L., and Solomon N.A. (Eds), The Benjamin/Cummings Publishing Company Inc., California
    • Kinoshita S. Glutamic acid bacteria. In: Demain A.L., and Solomon N.A. (Eds). Biology of Industrial Microorganisms (1985), The Benjamin/Cummings Publishing Company Inc., California 115-142
    • (1985) Biology of Industrial Microorganisms , pp. 115-142
    • Kinoshita, S.1
  • 2
    • 0033951735 scopus 로고    scopus 로고
    • Microbial biotechnology
    • Demain A.L. Microbial biotechnology. Trends Biotechnol. 18 (2000) 26-31
    • (2000) Trends Biotechnol. , vol.18 , pp. 26-31
    • Demain, A.L.1
  • 3
    • 0037271033 scopus 로고    scopus 로고
    • Amino acid production processes
    • Faurie R., and Thommel J. (Eds), Springer-Verlag, Berlin, Heidelberg
    • Ikeda M. Amino acid production processes. In: Faurie R., and Thommel J. (Eds). Adv. Biochem. Eng. Biotechnol.: Microbial Production of l-Amino Acids 79 (2003), Springer-Verlag, Berlin, Heidelberg 1-35
    • (2003) Adv. Biochem. Eng. Biotechnol.: Microbial Production of l-Amino Acids , vol.79 , pp. 1-35
    • Ikeda, M.1
  • 4
    • 0027513393 scopus 로고
    • Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I
    • Omori K., Imai Y., Suzuki S., and Komatsubara S. Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I. J. Bacterial. 175 (1993) 785-794
    • (1993) J. Bacterial. , vol.175 , pp. 785-794
    • Omori, K.1    Imai, Y.2    Suzuki, S.3    Komatsubara, S.4
  • 5
    • 0035405620 scopus 로고    scopus 로고
    • Overproduction of l-lysine from methanol by Methylobacillus glycogens
    • Motoyama H., Yano H., Terasaki T., and Anazawa H. Overproduction of l-lysine from methanol by Methylobacillus glycogens. Appl. Environ. Microbiol. 67 (2001) 3064-3070
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3064-3070
    • Motoyama, H.1    Yano, H.2    Terasaki, T.3    Anazawa, H.4
  • 6
    • 0036161274 scopus 로고    scopus 로고
    • A novel methodology employing Corynebacterium glutamicum genome information to generate a new l-lysine-producing mutant
    • Ohnishi J., Mitsuhashi S., Hayashi M., Ando S., Yokoi H., Ochiai K., and Ikeda M. A novel methodology employing Corynebacterium glutamicum genome information to generate a new l-lysine-producing mutant. Appl. Microbiol. Biotechnol. 58 (2002) 217-223
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 217-223
    • Ohnishi, J.1    Mitsuhashi, S.2    Hayashi, M.3    Ando, S.4    Yokoi, H.5    Ochiai, K.6    Ikeda, M.7
  • 7
    • 11144261828 scopus 로고    scopus 로고
    • A novel gnd mutation leading to increased l-lysine production in Corynebacterium glutamicum
    • Ohnishi J., Katahira R., Mitsuhashi S., Kakita S., and Ikeda M. A novel gnd mutation leading to increased l-lysine production in Corynebacterium glutamicum. FEMS Microbiol. Lett. 242 (2005) 265-274
    • (2005) FEMS Microbiol. Lett. , vol.242 , pp. 265-274
    • Ohnishi, J.1    Katahira, R.2    Mitsuhashi, S.3    Kakita, S.4    Ikeda, M.5
  • 8
    • 0028072688 scopus 로고
    • Detection and classification of mutagens: a set of base-specific Salmonella tester strains
    • Gee P., Maron D.M., and Ames B.N. Detection and classification of mutagens: a set of base-specific Salmonella tester strains. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 11606-11610
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11606-11610
    • Gee, P.1    Maron, D.M.2    Ames, B.N.3
  • 10
    • 0027513038 scopus 로고
    • Cloning of the trp gene cluster from a tryptophan-hyperproducing strain of Corynebacterium glutamicum: identification of a mutation in the trp leader sequence
    • Herry D.M., and Dunican L.K. Cloning of the trp gene cluster from a tryptophan-hyperproducing strain of Corynebacterium glutamicum: identification of a mutation in the trp leader sequence. Appl. Environ. Microbiol. 59 (1993) 791-799
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 791-799
    • Herry, D.M.1    Dunican, L.K.2
  • 12
    • 0037804190 scopus 로고    scopus 로고
    • A single V317A or V317M substitution in enzyme II of a newly identified β-glucoside phosphotransferase and utilization system of Corynebacterium glutamicum R extends its specificity towards cellobiose
    • Kotrba P., Inui M., and Yukawa H. A single V317A or V317M substitution in enzyme II of a newly identified β-glucoside phosphotransferase and utilization system of Corynebacterium glutamicum R extends its specificity towards cellobiose. Microbiology 149 (2003) 1569-1580
    • (2003) Microbiology , vol.149 , pp. 1569-1580
    • Kotrba, P.1    Inui, M.2    Yukawa, H.3
  • 13
    • 0035165362 scopus 로고    scopus 로고
    • Serine 187 is a crucial residue for allosteric regulation of Corynebacterium glutamicum 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase
    • Liao H., Lin L., Chien H.R., and Hsu W. Serine 187 is a crucial residue for allosteric regulation of Corynebacterium glutamicum 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase. FEMS Micobiol. Lett. 194 (2001) 59-64
    • (2001) FEMS Micobiol. Lett. , vol.194 , pp. 59-64
    • Liao, H.1    Lin, L.2    Chien, H.R.3    Hsu, W.4
  • 14
    • 0025247709 scopus 로고
    • Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase
    • Thierbach G., Kalinowski J., Bachmann B., and Pühler A. Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase. Appl. Microbiol. Biotechnol. 32 (1990) 443-448
    • (1990) Appl. Microbiol. Biotechnol. , vol.32 , pp. 443-448
    • Thierbach, G.1    Kalinowski, J.2    Bachmann, B.3    Pühler, A.4
  • 15
    • 0023445515 scopus 로고
    • Two single-base-pair substitutions causing desensitization to tryptophan feedback inhibition of anthranilate synthase and enhanced expression of tryptophan genes of Brevibacterium lactofermentum
    • Matsui K., Miwa K., and Sano K. Two single-base-pair substitutions causing desensitization to tryptophan feedback inhibition of anthranilate synthase and enhanced expression of tryptophan genes of Brevibacterium lactofermentum. J. Bacteriol. 169 (1987) 5330-5332
    • (1987) J. Bacteriol. , vol.169 , pp. 5330-5332
    • Matsui, K.1    Miwa, K.2    Sano, K.3
  • 16
    • 8644278779 scopus 로고    scopus 로고
    • Roles of pyruvate kinase and malic enzyme in Corynebacterium glutamicum for growth on carbon sources requiring gluconeogenesis
    • Netzer R., Krause M., Rittmann D., Peters-Wendish P.G., Eggeling L., Wendish V.F., and Sahm H. Roles of pyruvate kinase and malic enzyme in Corynebacterium glutamicum for growth on carbon sources requiring gluconeogenesis. Arch. Microbiol. 182 (2004) 354-363
    • (2004) Arch. Microbiol. , vol.182 , pp. 354-363
    • Netzer, R.1    Krause, M.2    Rittmann, D.3    Peters-Wendish, P.G.4    Eggeling, L.5    Wendish, V.F.6    Sahm, H.7
  • 17
    • 0031001311 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase of Escherichia coli
    • Kikuchi Y., Tsujimoto K., and Kurahashi O. Mutational analysis of the feedback sites of phenylalanine-sensitive 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase of Escherichia coli. Appl. Environ. Microbiol. 63 (1997) 761-762
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 761-762
    • Kikuchi, Y.1    Tsujimoto, K.2    Kurahashi, O.3
  • 18
    • 0026572565 scopus 로고
    • Analysis of the mutant proBA operon from a proline-producing strain of Serratia marcescens
    • Omori K., Suzuki S., Imai K., and Komatsubara S. Analysis of the mutant proBA operon from a proline-producing strain of Serratia marcescens. J. Gen. Microbiol. 138 (1992) 693-699
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 693-699
    • Omori, K.1    Suzuki, S.2    Imai, K.3    Komatsubara, S.4
  • 19
    • 0042162924 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum genome: features and impacts on biotechnological processes
    • Ikeda M., and Nakagawa S. The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl. Microbiol. Biotechnol. 62 (2003) 99-109
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 99-109
    • Ikeda, M.1    Nakagawa, S.2
  • 20
    • 33646163446 scopus 로고    scopus 로고
    • Comparisons of potentials for l-lysine production among different Corynebacterium glutamicum strains
    • Ohnishi J., and Ikeda M. Comparisons of potentials for l-lysine production among different Corynebacterium glutamicum strains. Biosci. Biotechnol. Biochem. 70 (2006) 1017-1020
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1017-1020
    • Ohnishi, J.1    Ikeda, M.2
  • 21
    • 33745013345 scopus 로고    scopus 로고
    • A genome-based approach to create a minimally mutated Corynebacterium glutamicum strain for efficient l-lysine production
    • Ikeda M., Ohnishi J., Hayashi M., and Mitsuhashi S. A genome-based approach to create a minimally mutated Corynebacterium glutamicum strain for efficient l-lysine production. J. Ind. Microbiol. Biotechnol. 33 (2006) 610-615
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 610-615
    • Ikeda, M.1    Ohnishi, J.2    Hayashi, M.3    Mitsuhashi, S.4
  • 22
    • 33751394915 scopus 로고    scopus 로고
    • Disruption of malate:quinone oxidoreductase increases l-lysine production by Corynebacterium glutamicum
    • Mitsuhashi S., Hayashi M., Ohnishi J., and Ikeda M. Disruption of malate:quinone oxidoreductase increases l-lysine production by Corynebacterium glutamicum. Biosci. Biotechnol. Biochem. 70 (2006) 2803-2806
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 2803-2806
    • Mitsuhashi, S.1    Hayashi, M.2    Ohnishi, J.3    Ikeda, M.4
  • 23
    • 33749007915 scopus 로고    scopus 로고
    • A leuC mutation leading to increased l-lysine production and rel-independent global expression changes in Corynebacterium glutamicum
    • Hayashi M., Mizoguchi H., Ohnishi J., Mitsuhashi S., Yonetani Y., Hashimoto S., and Ikeda M. A leuC mutation leading to increased l-lysine production and rel-independent global expression changes in Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 72 (2006) 783-789
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 783-789
    • Hayashi, M.1    Mizoguchi, H.2    Ohnishi, J.3    Mitsuhashi, S.4    Yonetani, Y.5    Hashimoto, S.6    Ikeda, M.7
  • 24
    • 0024847584 scopus 로고
    • l-Lysine production in continuous culture of an l-lysine hyperproducing mutant of Corynebacterium glutamicum
    • Hirao T., Nakano T., Azuma T., Sugimoto M., and Nakanishi T. l-Lysine production in continuous culture of an l-lysine hyperproducing mutant of Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 32 (1989) 269-273
    • (1989) Appl. Microbiol. Biotechnol. , vol.32 , pp. 269-273
    • Hirao, T.1    Nakano, T.2    Azuma, T.3    Sugimoto, M.4    Nakanishi, T.5
  • 25
    • 0028556301 scopus 로고
    • Transport of aromatic amino acids and its influence on overproduction of the amino acids in Corynebacterium glutamicum
    • Ikeda M., and Katsumata R. Transport of aromatic amino acids and its influence on overproduction of the amino acids in Corynebacterium glutamicum. J. Ferment. Bioeng. 78 (1994) 420-425
    • (1994) J. Ferment. Bioeng. , vol.78 , pp. 420-425
    • Ikeda, M.1    Katsumata, R.2
  • 26
    • 34250628080 scopus 로고    scopus 로고
    • Anaerobic growth and potential for amino acid production by nitrate respiration in Corynebacterium glutamicum
    • Takeno S., Ohnishi J., Komatsu T., Masaki T., Sen K., and Ikeda M. Anaerobic growth and potential for amino acid production by nitrate respiration in Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 75 (2007) 1173-1182
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 1173-1182
    • Takeno, S.1    Ohnishi, J.2    Komatsu, T.3    Masaki, T.4    Sen, K.5    Ikeda, M.6
  • 28
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito H., and Miura K. Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochem. Biophys. Acta 72 (1963) 619-629
    • (1963) Biochem. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 29
    • 0021278824 scopus 로고
    • Protoplast transformation of glutamate-producing bacteria with plasmid DNA
    • Katsumata R., Ozaki A., Oka T., and Furuya A. Protoplast transformation of glutamate-producing bacteria with plasmid DNA. J. Bacteriol. 159 (1984) 306-311
    • (1984) J. Bacteriol. , vol.159 , pp. 306-311
    • Katsumata, R.1    Ozaki, A.2    Oka, T.3    Furuya, A.4
  • 30
    • 36849073253 scopus 로고    scopus 로고
    • M. Ikeda, T. Nakano, S. Mitsuhashi, M. Hayashi, K. Tanaka, Method of producing l-arginine, l-ornithine, or l-citrulline, WO 2006/035831 A1, 2006.


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