메뉴 건너뛰기




Volumn 179, Issue 1, 1997, Pages 194-201

Bradyrhizobium japonicum does not require α-ketoglutarate dehydrogenase for growth on succinate or malate

Author keywords

[No Author keywords available]

Indexed keywords

MALIC ACID; OXOGLUTARATE DEHYDROGENASE; SUCCINIC ACID;

EID: 0031029980     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.1.194-201.1997     Document Type: Article
Times cited : (31)

References (47)
  • 1
    • 0025790990 scopus 로고
    • Cloning, sequencing, and mutational analysis of the Bradyrhizobium japonicum fumC-like gene: Evidence for the existence of two different fumarases
    • Acuña, G., S. Ebeling, and H. Hennecke. 1991. Cloning, sequencing, and mutational analysis of the Bradyrhizobium japonicum fumC-like gene: evidence for the existence of two different fumarases. J. Gen. Microbiol. 137:991-1000.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 991-1000
    • Acuña, G.1    Ebeling, S.2    Hennecke, H.3
  • 2
    • 0019354993 scopus 로고
    • Generation of succinyl-coenzyme A in photosynthetic bacteria
    • Beatty, T., and H. Gest. 1981. Generation of succinyl-coenzyme A in photosynthetic bacteria. Arch. Microbiol. 129:335-340.
    • (1981) Arch. Microbiol. , vol.129 , pp. 335-340
    • Beatty, T.1    Gest, H.2
  • 3
    • 0019778055 scopus 로고
    • Biosynthetic and bioenergetic functions of citric acid cycle reactions in Rhodopseudomonas capsulata
    • Beatty, T., and H. Gest. 1981. Biosynthetic and bioenergetic functions of citric acid cycle reactions in Rhodopseudomonas capsulata. J. Bacteriol. 148:584-593.
    • (1981) J. Bacteriol. , vol.148 , pp. 584-593
    • Beatty, T.1    Gest, H.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0025887460 scopus 로고
    • Development of the legume root nodule
    • Brewin, N. J. 1991. Development of the legume root nodule. Annu. Rev. Cell Biol. 7:191-226.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 191-226
    • Brewin, N.J.1
  • 6
    • 0021943866 scopus 로고
    • Supercoil sequencing: A fast and simple method for sequencing plasmid DNA
    • Chen, E. Y., and P. H. Seeburg. 1985. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA 4:165-170.
    • (1985) DNA , vol.4 , pp. 165-170
    • Chen, E.Y.1    Seeburg, P.H.2
  • 7
    • 0022393404 scopus 로고
    • Cyanobacterial light-harvesting complex subunits encoded in two red light-induced transcripts
    • Conley, P. B., P. G. Lemaux, and A. R. Grossman. 1985. Cyanobacterial light-harvesting complex subunits encoded in two red light-induced transcripts. Science 230:550-553.
    • (1985) Science , vol.230 , pp. 550-553
    • Conley, P.B.1    Lemaux, P.G.2    Grossman, A.R.3
  • 8
    • 0021447442 scopus 로고
    • Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12
    • Darlison, M. G., M. E. Spencer, and J. R. Guest. 1984. Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. Eur. J. Biochem. 141:351-359.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 351-359
    • Darlison, M.G.1    Spencer, M.E.2    Guest, J.R.3
  • 9
    • 0001904522 scopus 로고
    • Assay methods for key enzymes of the glyoxylate cycle
    • Dixon, G. H., and H. L. Kornberg. 1959. Assay methods for key enzymes of the glyoxylate cycle. Biochem. J. 72:3P.
    • (1959) Biochem. J. , vol.72
    • Dixon, G.H.1    Kornberg, H.L.2
  • 10
    • 0018411861 scopus 로고
    • α-Ketoglutarate dehydrogenase mutant of Rhizobium meliloti
    • Duncan, M. J., and D. G. Fraenkel. 1979. α-Ketoglutarate dehydrogenase mutant of Rhizobium meliloti. J. Bacteriol. 137:414-419.
    • (1979) J. Bacteriol. , vol.137 , pp. 414-419
    • Duncan, M.J.1    Fraenkel, D.G.2
  • 11
    • 0014273491 scopus 로고
    • Analysis of sporulation mutants. II. Mutants blocked in the citric acid cycle
    • Fortnagel, P., and E. Freese. 1968. Analysis of sporulation mutants. II. Mutants blocked in the citric acid cycle. J. Bacteriol. 95:1431-1438.
    • (1968) J. Bacteriol. , vol.95 , pp. 1431-1438
    • Fortnagel, P.1    Freese, E.2
  • 12
    • 0020429966 scopus 로고
    • Construction of a broad host range cosmid cloning vector and its use in the genetic analysis of Rhizobium mutants
    • Friedman, A. M., S. R. Long, S. E. Brown, W. J. Buikema, and F. M. Ausubel. 1982. Construction of a broad host range cosmid cloning vector and its use in the genetic analysis of Rhizobium mutants. Gene 18:289-296.
    • (1982) Gene , vol.18 , pp. 289-296
    • Friedman, A.M.1    Long, S.R.2    Brown, S.E.3    Buikema, W.J.4    Ausubel, F.M.5
  • 13
    • 15644374018 scopus 로고    scopus 로고
    • Submitted for publication
    • 12a.Green, L. S., and D. W. Emerich. Submitted for publication.
    • Green, L.S.1    Emerich, D.W.2
  • 14
    • 0021328016 scopus 로고
    • Localized mutagenesis in Rhizobium japonicum
    • Hahn, M., and H. Hennecke. 1984. Localized mutagenesis in Rhizobium japonicum. Mol. Gen. Genet. 193:46-52.
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 46-52
    • Hahn, M.1    Hennecke, H.2
  • 15
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 16
    • 0014344705 scopus 로고
    • Biochemical and genetic studies with lysine + methionine mutants of Escherichia coli: Lipoic acid and α-ketoglutarate dehydrogenase-less mutants
    • Herbert, A. A., and J. R. Guest. 1968. Biochemical and genetic studies with lysine + methionine mutants of Escherichia coli: lipoic acid and α-ketoglutarate dehydrogenase-less mutants. J. Gen. Microbiol. 53:363-381.
    • (1968) J. Gen. Microbiol. , vol.53 , pp. 363-381
    • Herbert, A.A.1    Guest, J.R.2
  • 17
    • 0014673708 scopus 로고
    • Studies with α-ketoglutarate dehydrogenase mutants of Escherichia coli
    • Herbert, A. A., and J. R. Guest. 1969. Studies with α-ketoglutarate dehydrogenase mutants of Escherichia coli. Mol. Gen. Genet. 105:182-190.
    • (1969) Mol. Gen. Genet. , vol.105 , pp. 182-190
    • Herbert, A.A.1    Guest, J.R.2
  • 18
    • 1942530691 scopus 로고
    • Enzymes of γ-aminobutyrate metabolism (bacterial)
    • Jakoby, W. B. 1962. Enzymes of γ-aminobutyrate metabolism (bacterial). Methods Enzymol. 5:765-778.
    • (1962) Methods Enzymol. , vol.5 , pp. 765-778
    • Jakoby, W.B.1
  • 19
    • 0025276762 scopus 로고
    • 4-Aminobutyrate is not available to bacteroids of cowpea Rhizobium MNF2030 in snake bean nodules
    • Jin, H. N., M. J. Dilworth, and A. R. Glenn. 1990. 4-Aminobutyrate is not available to bacteroids of cowpea Rhizobium MNF2030 in snake bean nodules. Arch. Microbiol. 153:455-462.
    • (1990) Arch. Microbiol. , vol.153 , pp. 455-462
    • Jin, H.N.1    Dilworth, M.J.2    Glenn, A.R.3
  • 20
    • 0345510338 scopus 로고
    • Enzymes of the glyoxylate cycle in rhizobia and nodules of legumes
    • Johnson, G. V., H. J. Evans, and T. Ching. 1966. Enzymes of the glyoxylate cycle in rhizobia and nodules of legumes. Plant Physiol. 41:1330-1336.
    • (1966) Plant Physiol. , vol.41 , pp. 1330-1336
    • Johnson, G.V.1    Evans, H.J.2    Ching, T.3
  • 21
    • 0024686859 scopus 로고
    • Protein phosphorylation in Bradyrhizobium japonicum bacteroids and cultures
    • Karr, D. B., and D. W. Emerich. 1989. Protein phosphorylation in Bradyrhizobium japonicum bacteroids and cultures. J. Bacteriol. 171:3420-3426.
    • (1989) J. Bacteriol. , vol.171 , pp. 3420-3426
    • Karr, D.B.1    Emerich, D.W.2
  • 22
    • 0000270332 scopus 로고
    • Enzymes of the poly-β-hydroxybutyrate and citric acid cycles of Rhizobium japonicum bacteroids
    • Karr, D. B., J. K. Waters, F. Suzuki, and D. W. Emerich. 1984. Enzymes of the poly-β-hydroxybutyrate and citric acid cycles of Rhizobium japonicum bacteroids. Plant Physiol. 75:1158-1162.
    • (1984) Plant Physiol. , vol.75 , pp. 1158-1162
    • Karr, D.B.1    Waters, J.K.2    Suzuki, F.3    Emerich, D.W.4
  • 23
    • 0013894468 scopus 로고
    • The role and control of the glyoxylate cycle in Escherichia coli
    • Kornberg, H. L. 1966. The role and control of the glyoxylate cycle in Escherichia coli. Biochem. J. 99:1-11.
    • (1966) Biochem. J. , vol.99 , pp. 1-11
    • Kornberg, H.L.1
  • 24
    • 0007279185 scopus 로고
    • Uptake and metabolism of aspartate and glutamate by soybean nodule bacteroids
    • H. Bothe, F. de Bruijn, and W. E. Newton (ed.), Gustav Fischer, New York, N.Y.
    • Kouchi, H., and K. Fukai. 1988. Uptake and metabolism of aspartate and glutamate by soybean nodule bacteroids, p. 561. In H. Bothe, F. de Bruijn, and W. E. Newton (ed.), Nitrogen fixation: 100 years after. Gustav Fischer, New York, N.Y.
    • (1988) Nitrogen Fixation: 100 Years after , pp. 561
    • Kouchi, H.1    Fukai, K.2
  • 25
    • 0000684138 scopus 로고
    • Isolation and enzymological characterization of infected and uninfected cell protoplasts from root nodules of Glycine max
    • Kouchi, H., K. Fukai, H. Katagiri, K. Minamisawa, and S. Tajima. 1988. Isolation and enzymological characterization of infected and uninfected cell protoplasts from root nodules of Glycine max. Physiol. Plant. 73:327-334.
    • (1988) Physiol. Plant. , vol.73 , pp. 327-334
    • Kouchi, H.1    Fukai, K.2    Katagiri, H.3    Minamisawa, K.4    Tajima, S.5
  • 28
    • 0023231674 scopus 로고
    • Cluster of genes controlling synthesis and activation of 2-3-dihydroxybenzoic acid in production of enterobactin in Escherichia coli
    • Nahlik, M. S., T. P. Fleming, and M. A. McIntosh. 1987. Cluster of genes controlling synthesis and activation of 2-3-dihydroxybenzoic acid in production of enterobactin in Escherichia coli. J. Bacteriol. 169:4163-4170.
    • (1987) J. Bacteriol. , vol.169 , pp. 4163-4170
    • Nahlik, M.S.1    Fleming, T.P.2    McIntosh, M.A.3
  • 29
    • 0016192458 scopus 로고
    • L-Arabinose metabolism in Rhizobium japonicum
    • Pedroso, F. O., and G. T. Zancan. 1974. L-Arabinose metabolism in Rhizobium japonicum. J. Bacteriol. 119:336-338.
    • (1974) J. Bacteriol. , vol.119 , pp. 336-338
    • Pedroso, F.O.1    Zancan, G.T.2
  • 30
    • 0028341392 scopus 로고
    • Effects of organic acids and low pH on Rhizobium meliloti 104A14
    • Perez-Galdona, R., and M. L. Kahn. 1994. Effects of organic acids and low pH on Rhizobium meliloti 104A14, Microbiology 140:1231-1235.
    • (1994) Microbiology , vol.140 , pp. 1231-1235
    • Perez-Galdona, R.1    Kahn, M.L.2
  • 31
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxoglutarate dehydrogenase multienzyme complexes: A paradigm in the design of multifunctional protein
    • Perham, R. N. 1991. Domains, motifs, and linkers in 2-oxoglutarate dehydrogenase multienzyme complexes: a paradigm in the design of multifunctional protein. Biochemistry 30:8501-8512.
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 32
    • 0025830682 scopus 로고
    • Codon usage and G + C content in Bradyrhizobium japonicum genes are not uniform
    • Ramseier, T. M., and M. Göttfert. 1991. Codon usage and G + C content in Bradyrhizobium japonicum genes are not uniform. Arch. Microbiol. 156:270-276.
    • (1991) Arch. Microbiol. , vol.156 , pp. 270-276
    • Ramseier, T.M.1    Göttfert, M.2
  • 33
    • 77956995420 scopus 로고
    • α-Ketoglutarate dehydrogenase complex from Escherichia coli
    • Reed, L. J., and B. B. Mukherjee. 1969. α-Ketoglutarate dehydrogenase complex from Escherichia coli. Methods Enzymol. 13:55-61.
    • (1969) Methods Enzymol. , vol.13 , pp. 55-61
    • Reed, L.J.1    Mukherjee, B.B.2
  • 34
    • 0026662882 scopus 로고
    • Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex
    • Resnekov, O., L. Melin, F. Carlsson, M. Mannerlov, A. von Gabain, and L. Hederstedt. 1992. Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex. Mol. Gen. Genet. 234:285-296.
    • (1992) Mol. Gen. Genet. , vol.234 , pp. 285-296
    • Resnekov, O.1    Melin, L.2    Carlsson, F.3    Mannerlov, M.4    Von Gabain, A.5    Hederstedt, L.6
  • 35
    • 0025089232 scopus 로고
    • Factors contributing to the accumulation of glutamate in Bradyrhizobium joponicum bacteroids under microaerobic conditions
    • Salminen, S. O., and J. G. Streeter. 1990. Factors contributing to the accumulation of glutamate in Bradyrhizobium joponicum bacteroids under microaerobic conditions. J. Gen. Microbiol. 136:2119-2126.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2119-2126
    • Salminen, S.O.1    Streeter, J.G.2
  • 37
    • 0025021822 scopus 로고
    • The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component
    • Schulze, E., A. H. Westphal, R. Hanemaaijer, and A. de Kok. 1990. The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component. Eur. J. Biochem. 187:229-234.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 229-234
    • Schulze, E.1    Westphal, A.H.2    Hanemaaijer, R.3    De Kok, A.4
  • 38
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 39
    • 15644382655 scopus 로고
    • Mutant strains of Aerobacter aerogenes which require both methionine and lysine for aerobic growth
    • Stouthamer, A. H. 1967. Mutant strains of Aerobacter aerogenes which require both methionine and lysine for aerobic growth. J. Gen. Microbiol. 46:389-398.
    • (1967) J. Gen. Microbiol. , vol.46 , pp. 389-398
    • Stouthamer, A.H.1
  • 40
    • 0012853635 scopus 로고
    • Organic acid metabolism by isolated Rhizobium japonicum bacteroids
    • Stovall, I., and M. Cole. 1978. Organic acid metabolism by isolated Rhizobium japonicum bacteroids. Plant Physiol. 61:787-790.
    • (1978) Plant Physiol. , vol.61 , pp. 787-790
    • Stovall, I.1    Cole, M.2
  • 41
    • 77956846102 scopus 로고
    • Transport and metabolism of carbon and nitrogen in legume nodules
    • Streeter, J. G. 1991. Transport and metabolism of carbon and nitrogen in legume nodules. Adv. Bot. Res. 18:129-187.
    • (1991) Adv. Bot. Res. , vol.18 , pp. 129-187
    • Streeter, J.G.1
  • 42
    • 0017285746 scopus 로고
    • A biochemical basis for obligate methylotrophy: Properties of a mutant of Pseudomonas AM1 lacking 2-oxoglutarate dehydrogenase
    • Taylor, I. J., and C. Anthony. 1976. A biochemical basis for obligate methylotrophy: properties of a mutant of Pseudomonas AM1 lacking 2-oxoglutarate dehydrogenase. J. Gen. Microbiol. 93:259-265.
    • (1976) J. Gen. Microbiol. , vol.93 , pp. 259-265
    • Taylor, I.J.1    Anthony, C.2
  • 43
    • 0003728496 scopus 로고
    • International biological programme. Blackwell Scientific Publications, Oxford. United Kingdom
    • Vincent, J. M. 1970. A manual for the practical study of root-nodule bacteria. International biological programme. Blackwell Scientific Publications, Oxford. United Kingdom.
    • (1970) A Manual for the Practical Study of Root-nodule Bacteria
    • Vincent, J.M.1
  • 45
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way, J. C., M. A. Davis, D. Morisato, D. E. Roberts, and N. Kleckner. 1984. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32:369-379.
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5
  • 46
    • 0000477986 scopus 로고
    • Physiology of nitrogen-fixing legume nodules: Compartments and functions
    • G. Stacey, R. H. Burris, and H. J. Evans (ed.), Chapman and Hall, New York, N.Y.
    • Werner, D. 1992. Physiology of nitrogen-fixing legume nodules: compartments and functions, p. 399-431. In G. Stacey, R. H. Burris, and H. J. Evans (ed.), Biological nitrogen fixation. Chapman and Hall, New York, N.Y.
    • (1992) Biological Nitrogen Fixation , pp. 399-431
    • Werner, D.1
  • 47
    • 0001596005 scopus 로고
    • Poly-β-hydroxybutyrate utilization by soybean (Glycine max Merr.) nodules and assessment of its role in maintenance of nitrogenase activity
    • Wong, P. P., and H. J. Evans. 1971. Poly-β-hydroxybutyrate utilization by soybean (Glycine max Merr.) nodules and assessment of its role in maintenance of nitrogenase activity. Plant Physiol. 47:750-755.
    • (1971) Plant Physiol. , vol.47 , pp. 750-755
    • Wong, P.P.1    Evans, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.