메뉴 건너뛰기




Volumn 191, Issue 24, 2009, Pages 7581-7586

Deletion of citrate synthase restores growth of Sinorhizobium meliloti 1021 aconitase mutants

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; CITRATE SYNTHASE; IRON; ISOCITRATE DEHYDROGENASE;

EID: 72449149315     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00777-09     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 0033621064 scopus 로고    scopus 로고
    • Bacillus subtilis aconitase is an RNA-binding protein
    • Alen, C., and A. L. Sonenshein. 1999. Bacillus subtilis aconitase is an RNA-binding protein. Proc. Natl. Acad. Sci. USA 96:10412-10417.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10412-10417
    • Alen, C.1    Sonenshein, A.L.2
  • 2
    • 34249815828 scopus 로고    scopus 로고
    • Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase
    • Banerjee, S., A. K. Nandyala, P. Raviprasad, N. Ahmed, and S. E. Hasnain. 2007. Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase. J. Bacteriol. 189:4046-4052.
    • (2007) J. Bacteriol. , vol.189 , pp. 4046-4052
    • Banerjee, S.1    Nandyala, A.K.2    Raviprasad, P.3    Ahmed, N.4    Hasnain, S.E.5
  • 3
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein
    • Beinert, H., M. C. Kennedy, and C. D. Stout. 1996. Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein. Chem. Rev. 96:2335-2374.
    • (1996) Chem. Rev. , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 4
    • 0016231913 scopus 로고
    • R factor transfer in Rhizobium leguminosarum
    • Beringer, J. E. 1974. R factor transfer in Rhizobium leguminosarum. J. Gen. Microbiol. 84:188-198.
    • (1974) J. Gen. Microbiol. , vol.84 , pp. 188-198
    • Beringer, J.E.1
  • 6
    • 0030726675 scopus 로고    scopus 로고
    • A null mutation in the Bacillus subtilis aconitase gene causes a block in Spo0A-phosphate- Dependent gene expression
    • Craig, J. E., M. J. Ford, D. C. Blaydon, and A. L. Sonenshein. 1997. A null mutation in the Bacillus subtilis aconitase gene causes a block in Spo0A-phosphate- dependent gene expression. J. Bacteriol. 179:7351-7359.
    • (1997) J. Bacteriol. , vol.179 , pp. 7351-7359
    • Craig, J.E.1    Ford, M.J.2    Blaydon, D.C.3    Sonenshein, A.L.4
  • 7
    • 0027390501 scopus 로고
    • Analysis of Pseudomonas gene products using lacI(q)/Ptrp-lac plasmids and transposons that confer conditional phenotypes
    • DOI 10.1016/0378-1119(93)90533-9
    • de Lorenzo, V., L. Eltis, B. Kessler, and K. N. Timmis. 1993. Analysis of Pseudomonas gene products using lacIq/Ptrp-lac plasmids and transposons that confer conditional phenotypes. Gene 123:17-24. (Pubitemid 23035786)
    • (1993) Gene , vol.123 , Issue.1 , pp. 17-24
    • De Lorenzo, V.1    Eltis, L.2    Kessler, B.3    Timmis, K.N.4
  • 8
    • 0027416043 scopus 로고
    • NAD(+)-dependent malic enzyme of Rhizobium meliloti is required for symbiotic nitrogen fixation
    • Driscoll, B. T., and T. M. Finan. 1993. NAD(+)-dependent malic enzyme of Rhizobium meliloti is required for symbiotic nitrogen fixation. Mol. Microbiol. 7:865-873.
    • (1993) Mol. Microbiol. , vol.7 , pp. 865-873
    • Driscoll, B.T.1    Finan, T.M.2
  • 9
    • 0029949195 scopus 로고    scopus 로고
    • +-dependent malic enzyme of Rhizobium meliloti
    • +-dependent malic enzyme of Rhizobium meliloti. J. Bacteriol. 178:2224-2231.
    • (1996) J. Bacteriol. , vol.178 , pp. 2224-2231
    • Driscoll, B.T.1    Finan, T.M.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. 137:415-419.
    • (1979) J. Bacteriol. , vol.137 , pp. 415-419
    • Duncan, M.J.1    Fraenkel, D.G.2
  • 11
    • 8844253256 scopus 로고    scopus 로고
    • Insertion of transposon Tn5tac1 in the Sinorhizobium meliloti malate dehydrogenase (mdh) gene results in conditional polar effects on downstream TCA cycle genes
    • Dymov, S. L., D. J. J. Meek, B. Steven, and B. T. Driscoll. 2004. Insertion of transposon Tn5tac1 in the Sinorhizobium meliloti malate dehydrogenase (mdh) gene results in conditional polar effects on downstream TCA cycle genes. Mol. Plant-Microbe Interact. 17:1318-1327.
    • (2004) Mol. Plant-Microbe Interact. , vol.17 , pp. 1318-1327
    • Dymov, S.L.1    Meek, D.J.J.2    Steven, B.3    Driscoll, B.T.4
  • 12
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and D. R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. USA 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 15
    • 0030748655 scopus 로고    scopus 로고
    • Construction and properties of aconitase mutants of Escherichia coli
    • Gruer, M. J., A. J. Bradbury, and J. R. Guest. 1997. Construction and properties of aconitase mutants of Escherichia coli. Microbiology 143:1837-1846. (Pubitemid 27290272)
    • (1997) Microbiology , vol.143 , Issue.6 , pp. 1837-1846
    • Gruer, M.J.1    Bradbury, A.J.2    Guest, J.R.3
  • 16
    • 12444338966 scopus 로고    scopus 로고
    • Probing the Sinorhizobium meliloti-alfalfa symbiosis using temperature-sensitive and impairedfunction citrate synthase mutants
    • Grzemski, W., J. P. Akowski, and M. L. Kahn. 2005. Probing the Sinorhizobium meliloti-alfalfa symbiosis using temperature-sensitive and impairedfunction citrate synthase mutants. Mol. Plant-Microbe Interact. 18:134-141.
    • (2005) Mol. Plant-Microbe Interact. , vol.18 , pp. 134-141
    • Grzemski, W.1    Akowski, J.P.2    Kahn, M.L.3
  • 17
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 18
    • 2442646859 scopus 로고    scopus 로고
    • New recombination methods for Sinorhizobium meliloti genetics
    • House, B. L., M. W. Mortimer, and M. L. Kahn. 2004. New recombination methods for Sinorhizobium meliloti genetics. Appl. Environ. Microbiol. 70: 2806-2815.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2806-2815
    • House, B.L.1    Mortimer, M.W.2    Kahn, M.L.3
  • 20
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R. A., T. A. Kavanagh, and M. W. Bevan. 1987. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6:3901-3907.
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 22
    • 0021112587 scopus 로고
    • The role of iron in the activation-inactivation of aconitase
    • Kennedy, M. C., M. H. Emptage, J. L. Dreyer, and H. Beinert. 1983. The role of iron in the activation-inactivation of aconitase. J. Biol. Chem. 258:11098-11105.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11098-11105
    • Kennedy, M.C.1    Emptage, M.H.2    Dreyer, J.L.3    Beinert, H.4
  • 23
    • 0027081042 scopus 로고
    • Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein
    • Kennedy, M. C., L. Mende-Mueller, G. A. Blondin, and H. Beinert. 1992. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci. USA 89:11730-11734.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11730-11734
    • Kennedy, M.C.1    Mende-Mueller, L.2    Blondin, G.A.3    Beinert, H.4
  • 24
    • 43949119420 scopus 로고    scopus 로고
    • Suppression of metabolic defects of yeast isocitrate dehydrogenase and aconitase mutants by loss of citrate synthase
    • Lin, A. P., K. W. Hakala, S. T. Weintraub, and L. McAlister-Henn. 2008. Suppression of metabolic defects of yeast isocitrate dehydrogenase and aconitase mutants by loss of citrate synthase. Arch. Biochem. Biophys. 474:205-212.
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 205-212
    • Lin, A.P.1    Hakala, K.W.2    Weintraub, S.T.3    McAlister-Henn, L.4
  • 25
    • 0026710389 scopus 로고
    • Cloning and mutagenesis of the Rhizobium meliloti isocitrate dehydrogenase gene
    • McDermott, T. R., and M. L. Kahn. 1992. Cloning and mutagenesis of the Rhizobium meliloti isocitrate dehydrogenase gene. J. Bacteriol. 174:4790-4797.
    • (1992) J. Bacteriol. , vol.174 , pp. 4790-4797
    • McDermott, T.R.1    Kahn, M.L.2
  • 26
    • 0020058862 scopus 로고
    • Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis
    • Meade, H. M., S. R. Long, G. B. Ruvkun, S. E. Brown, and F. M. Ausubel. 1982. Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis. J. Bacteriol. 149:114-122.
    • (1982) J. Bacteriol. , vol.149 , pp. 114-122
    • Meade, H.M.1    Long, S.R.2    Ruvkun, G.B.3    Brown, S.E.4    Ausubel, F.M.5
  • 27
    • 0032779109 scopus 로고    scopus 로고
    • Citrate synthase mutants of Sinorhizobium meliloti are ineffective and have altered cell surface polysaccharides
    • Mortimer, M. W., T. R. McDermott, G. M. York, G. C. Walker, and M. L. Kahn. 1999. Citrate synthase mutants of Sinorhizobium meliloti are ineffective and have altered cell surface polysaccharides. J. Bacteriol. 181:7608-7613.
    • (1999) J. Bacteriol. , vol.181 , pp. 7608-7613
    • Mortimer, M.W.1    McDermott, T.R.2    York, G.M.3    Walker, G.C.4    Kahn, M.L.5
  • 28
    • 0030895301 scopus 로고    scopus 로고
    • Heme compounds as iron sources for nonpathogenic Rhizobium bacteria
    • Noya, F., A. Arias, and E. Fabiano. 1997. Heme compounds as iron sources for nonpathogenic Rhizobium bacteria. J. Bacteriol. 179:3076-3078.
    • (1997) J. Bacteriol. , vol.179 , pp. 3076-3078
    • Noya, F.1    Arias, A.2    Fabiano, E.3
  • 29
    • 3242774756 scopus 로고    scopus 로고
    • Fur is involved in manganese-dependent regulation of mntA (sitA) expression in Sinorhizobium meliloti
    • Platero, R., L. Peixoto, M. R. O'Brian, and E. Fabiano. 2004. Fur is involved in manganese-dependent regulation of mntA (sitA) expression in Sinorhizobium meliloti. Appl. Environ. Microbiol. 70:4349-4355.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 4349-4355
    • Platero, R.1    Peixoto, L.2    O'Brian, M.R.3    Fabiano, E.4
  • 30
    • 33947371689 scopus 로고    scopus 로고
    • Sinorhizobium meliloti pSymB carries genes necessary for arabinose transport and catabolism
    • Poysti, N. J., E. D. Loewen, Z. Wang, and I. J. Oresnik. 2007. Sinorhizobium meliloti pSymB carries genes necessary for arabinose transport and catabolism. Microbiology 153:727-736.
    • (2007) Microbiology , vol.153 , pp. 727-736
    • Poysti, N.J.1    Loewen, E.D.2    Wang, Z.3    Oresnik, I.J.4
  • 31
    • 0025943925 scopus 로고
    • The aconitase of Escherichia coli: Purification of the enzyme and molecular cloning and map location of the gene (acn)
    • Prodromou, C., M. J. Haynes, and J. R. Guest. 1991. The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn). J. Gen. Microbiol. 137:2505-2515.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2505-2515
    • Prodromou, C.1    Haynes, M.J.2    Guest, J.R.3
  • 32
    • 0014216603 scopus 로고
    • Mechanism of aconitase action. I. the hydrogen transfer reaction
    • Rose, I. A., and E. L. O'Connell. 1967. Mechanism of aconitase action. I. The hydrogen transfer reaction. J. Biol. Chem. 242:1870-1879.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1870-1879
    • Rose, I.A.1    O'Connell, E.L.2
  • 33
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • DOI 10.1016/0378-1119(94)90324-7
    • Schafer, A., A. Tauch, W. Jager, J. Kalinowski, G. Thierbach, and A. Puhler. 1994. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145:69-73. (Pubitemid 24224965)
    • (1994) Gene , vol.145 , Issue.1 , pp. 69-73
    • Schafer, A.1    Tauch, A.2    Jager, W.3    Kalinowski, J.4    Thierbach, G.5    Puhler, A.6
  • 35
    • 0024339688 scopus 로고
    • New derivatives of transposon Tn5 suitable for mobilization of replicons, generation of operon fusions and induction of genes in Gram-negative bacteria
    • DOI 10.1016/0378-1119(89)90262-X
    • Simon, R., J. Quandt, and W. Klipp. 1989. New derivatives of transposon Tn5 suitable for mobilization of replicons, generation of operon fusions and induction of genes in gram-negative bacteria. Gene 80:161-169. (Pubitemid 19192673)
    • (1989) Gene , vol.80 , Issue.1 , pp. 161-169
    • Simon, R.1    Quandt, J.2    Klipp, W.3
  • 36
    • 0033029088 scopus 로고    scopus 로고
    • Physiological characterization of Pseudomonas aeruginosa during exotoxin a synthesis: Glutamate, iron limitation, and aconitase activity
    • Somerville, G., C. A. Mikoryak, and L. Reitzer. 1999. Physiological characterization of Pseudomonas aeruginosa during exotoxin A synthesis: glutamate, iron limitation, and aconitase activity. J. Bacteriol. 181:1072-1078.
    • (1999) J. Bacteriol. , vol.181 , pp. 1072-1078
    • Somerville, G.1    Mikoryak, C.A.2    Reitzer, L.3
  • 37
    • 0021085146 scopus 로고
    • Cloning of the glutamine synthetase I gene from Rhizobium meliloti
    • Somerville, J. E., and M. L. Kahn. 1983. Cloning of the glutamine synthetase I gene from Rhizobium meliloti. J. Bacteriol. 156:168-176.
    • (1983) J. Bacteriol. , vol.156 , pp. 168-176
    • Somerville, J.E.1    Kahn, M.L.2
  • 38
    • 0032739921 scopus 로고    scopus 로고
    • Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
    • Tang, Y., and J. R. Guest. 1999. Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 145:3069-3079. (Pubitemid 29535027)
    • (1999) Microbiology , vol.145 , Issue.11 , pp. 3069-3079
    • Tang, Y.1    Guest, J.R.2
  • 39
    • 1642565352 scopus 로고    scopus 로고
    • Post-transcriptional regulation of bacterial motility by aconitase proteins
    • Tang, Y., J. R. Guest, P. J. Artymiuk, R. C. Read, and J. Green. 2004. Post-transcriptional regulation of bacterial motility by aconitase proteins. Mol. Microbiol. 51:1817-1826.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1817-1826
    • Tang, Y.1    Guest, J.R.2    Artymiuk, P.J.3    Read, R.C.4    Green, J.5
  • 40
    • 0036225829 scopus 로고    scopus 로고
    • Escherichia coli aconitases and oxidative stress: Post-transcriptional regulation of sodA expression
    • Tang, Y., M. A. Quail, P. J. Artymiuk, J. R. Guest, and J. Green. 2002. Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology 148:1027-1037. (Pubitemid 34436778)
    • (2002) Microbiology , vol.148 , Issue.4 , pp. 1027-1037
    • Tang, Y.1    Quail, M.A.2    Artymiuk, P.J.3    Guest, J.R.4    Green, J.5
  • 41
    • 0029967017 scopus 로고    scopus 로고
    • The Bradyrhizobium japonicum aconitase gene (acnA) is important for free-living growth but not for an effective root nodule symbiosis
    • Thony-Meyer, L., and P. Kunzler. 1996. The Bradyrhizobium japonicum aconitase gene (acnA) is important for free-living growth but not for an effective root nodule symbiosis. J. Bacteriol. 178:6166-6172.
    • (1996) J. Bacteriol. , vol.178 , pp. 6166-6172
    • Thony-Meyer, L.1    Kunzler, P.2
  • 42
    • 0034824911 scopus 로고    scopus 로고
    • Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus acidocaldarius
    • Uhrigshardt, H., M. Walden, H. John, and S. Anemuller. 2001. Purification and characterization of the first archaeal aconitase from the thermoacidophilic Sulfolobus acidocaldarius. Eur. J. Biochem. 268:1760-1771.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1760-1771
    • Uhrigshardt, H.1    Walden, M.2    John, H.3    Anemuller, S.4
  • 43
    • 0035030167 scopus 로고    scopus 로고
    • Roles of aconitase in growth, metabolism, and morphological differentiation of Streptomyces coelicolor
    • Viollier, P. H., K. T. Nguyen, W. Minas, M. Folcher, G. E. Dale, and C. J. Thompson. 2001. Roles of aconitase in growth, metabolism, and morphological differentiation of Streptomyces coelicolor. J. Bacteriol. 183:3193-3203.
    • (2001) J. Bacteriol. , vol.183 , pp. 3193-3203
    • Viollier, P.H.1    Nguyen, K.T.2    Minas, W.3    Folcher, M.4    Dale, G.E.5    Thompson, C.J.6
  • 44
    • 0031807487 scopus 로고    scopus 로고
    • The rpfA gene of Xanthomonas campestris pathovar campestris, which is involved in the regulation of pathogenicity factor production, encodes an aconitase
    • Wilson, T. J., N. Bertrand, J. L. Tang, J. X. Feng, M. Q. Pan, C. E. Barber, J. M. Dow, and M. J. Daniels. 1998. The rpfA gene of Xanthomonas campestris pathovar campestris, which is involved in the regulation of pathogenicity factor production, encodes an aconitase. Mol. Microbiol. 28:961-970.
    • (1998) Mol. Microbiol. , vol.28 , pp. 961-970
    • Wilson, T.J.1    Bertrand, N.2    Tang, J.L.3    Feng, J.X.4    Pan, M.Q.5    Barber, C.E.6    Dow, J.M.7    Daniels, M.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.