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Volumn 179, Issue 17, 1997, Pages 5516-5520

Metals control activity and expression of the heme biosynthesis enzyme δ-aminolevulinic acid dehydratase in Bradyrhizobium japonicum

Author keywords

[No Author keywords available]

Indexed keywords

METAL; PORPHOBILINOGEN SYNTHASE;

EID: 0030885964     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.17.5516-5520.1997     Document Type: Article
Times cited : (32)

References (28)
  • 1
    • 0000462106 scopus 로고
    • The origin and functions of haemoglobins in plants
    • Appleby, C. A. 1992. The origin and functions of haemoglobins in plants. Sci. Prog. Oxf. 76:365-398.
    • (1992) Sci. Prog. Oxf. , vol.76 , pp. 365-398
    • Appleby, C.A.1
  • 3
    • 85011571950 scopus 로고
    • Genetics of bacterial iron transport
    • G. Winkelmann (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Braun, V., and V. Hantke. 1991. Genetics of bacterial iron transport, p. 107-138. In G. Winkelmann (ed.), CRC handbook of microbial iron chelates. CRC Press, Inc., Boca Raton, Fla.
    • (1991) CRC Handbook of Microbial Iron Chelates , pp. 107-138
    • Braun, V.1    Hantke, V.2
  • 4
    • 0027432041 scopus 로고
    • Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain
    • Chauhan, S., and M. R. O'Brian. 1993. Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain. J. Bacteriol. 175:7222-7227.
    • (1993) J. Bacteriol. , vol.175 , pp. 7222-7227
    • Chauhan, S.1    O'Brian, M.R.2
  • 5
    • 0029121431 scopus 로고
    • A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules
    • Chauhan, S., and M. R. O'Brian. 1995. A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules. J. Biol. Chem. 270:19823-19827.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19823-19827
    • Chauhan, S.1    O'Brian, M.R.2
  • 6
    • 0031007110 scopus 로고    scopus 로고
    • Transcriptional regulation of δ-aminolevulinic acid dehydratase by oxygen in Bradyrhizobium japonicum and evidence for developmental control of the hemB gene
    • Chauhan, S., and M. R. O'Brian. 1997. Transcriptional regulation of δ-aminolevulinic acid dehydratase by oxygen in Bradyrhizobium japonicum and evidence for developmental control of the hemB gene. J. Bacteriol. 179: 3706-3710.
    • (1997) J. Bacteriol. , vol.179 , pp. 3706-3710
    • Chauhan, S.1    O'Brian, M.R.2
  • 7
    • 0025811624 scopus 로고
    • Human erythroid δ-aminolevulinic acid synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • Cox, T. C., M. J. Bawden, A. Martin, and B. K. May. 1991. Human erythroid δ-aminolevulinic acid synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 10:1891-1902.
    • (1991) EMBO J. , vol.10 , pp. 1891-1902
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 8
    • 0028047783 scopus 로고
    • Human ferrochelatase is an iron-sulfur protein
    • Dailey, H. A., M. G. Finnegan, and M. K. Johnson. 1994. Human ferrochelatase is an iron-sulfur protein. Biochemistry 33:403-407.
    • (1994) Biochemistry , vol.33 , pp. 403-407
    • Dailey, H.A.1    Finnegan, M.G.2    Johnson, M.K.3
  • 9
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid δ-aminolevulinic acid synthase mRNA
    • Handekar, T., R. Stripecke, N. K. Gray, B. Goossen, A. Constable, H. E. Johansson, and M. W. Hentze. 1991. Identification of a novel iron-responsive element in murine and human erythroid δ-aminolevulinic acid synthase mRNA. EMBO J. 10:1903-1909.
    • (1991) EMBO J. , vol.10 , pp. 1903-1909
    • Handekar, T.1    Stripecke, R.2    Gray, N.K.3    Goossen, B.4    Constable, A.5    Johansson, H.E.6    Hentze, M.W.7
  • 10
    • 0025171361 scopus 로고
    • Two different zinc sites in bovine 5-aminolevulinate dehydratase distinguished by extended X-ray absorption fine structure
    • Dent, A. J., D. Beyersmann, C. Block, and S. S. Hasnain. 1990. Two different zinc sites in bovine 5-aminolevulinate dehydratase distinguished by extended X-ray absorption fine structure. Biochemistry 29:7822-7828.
    • (1990) Biochemistry , vol.29 , pp. 7822-7828
    • Dent, A.J.1    Beyersmann, D.2    Block, C.3    Hasnain, S.S.4
  • 12
    • 0026766340 scopus 로고
    • Rhizobium-plant signal exchange
    • Fisher, R. F., and S. R. Long. 1992. Rhizobium-plant signal exchange. Nature 357:655-660.
    • (1992) Nature , vol.357 , pp. 655-660
    • Fisher, R.F.1    Long, S.R.2
  • 13
    • 0026665634 scopus 로고
    • Characterization of a Bradyrhizobium japonicum ferrochelatase mutant and isolation of the hemH gene
    • Frustaci, J. M., and M. R. O'Brian. 1992. Characterization of a Bradyrhizobium japonicum ferrochelatase mutant and isolation of the hemH gene. J. Bacteriol. 174:4223-4229.
    • (1992) J. Bacteriol. , vol.174 , pp. 4223-4229
    • Frustaci, J.M.1    O'Brian, M.R.2
  • 14
    • 0026071003 scopus 로고
    • Aerobic growth and respiration of a δ-aminolevulinic acid (hemA) mutant of Bradyrhizobium japonicum
    • Frustaci, J. M., I. Sangwan, and M. R. O'Brian. 1991. Aerobic growth and respiration of a δ-aminolevulinic acid (hemA) mutant of Bradyrhizobium japonicum. J. Bacteriol. 173:1145-1150.
    • (1991) J. Bacteriol. , vol.173 , pp. 1145-1150
    • Frustaci, J.M.1    Sangwan, I.2    O'Brian, M.R.3
  • 15
    • 0342389494 scopus 로고
    • 65Zinc binding and exchange with enzyme from human erythrocytes
    • 65Zinc binding and exchange with enzyme from human erythrocytes. Biochem. Soc. Trans. 9:232-233.
    • (1981) Biochem. Soc. Trans. , vol.9 , pp. 232-233
    • Gibbs, P.N.B.1    Jordan, P.M.2
  • 16
    • 0022516509 scopus 로고
    • Bacterial δ-aminolevulinic acid synthase activity is not essential for leghemoglobin formation in the soybean/ Bradyrhizobium japonicum symbiosis
    • Guerinot, M. L., and B. K. Chelm. 1986. Bacterial δ-aminolevulinic acid synthase activity is not essential for leghemoglobin formation in the soybean/ Bradyrhizobium japonicum symbiosis. Proc. Natl. Acad. Sci. USA 83:1837-1841.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1837-1841
    • Guerinot, M.L.1    Chelm, B.K.2
  • 17
    • 0002107398 scopus 로고
    • The role of respiration in symbiotic nitrogen fixation
    • R. Palacios, J. Mora, and W. E. Newton (ed.), Kluwer Academic, Boston, Mass.
    • Hennecke, H. 1993. The role of respiration in symbiotic nitrogen fixation, p. 55-64. In R. Palacios, J. Mora, and W. E. Newton (ed.), New horizons in nitrogen fixation. Kluwer Academic, Boston, Mass.
    • (1993) New Horizons in Nitrogen Fixation , pp. 55-64
    • Hennecke, H.1
  • 18
    • 0025779813 scopus 로고
    • Reevaluation of a sensitive indicator of early lead exposure. Measurement of porphobilinogen synthase in blood
    • Jaffe, E. K., S. Bagla, and P. A. Michini. 1991. Reevaluation of a sensitive indicator of early lead exposure. Measurement of porphobilinogen synthase in blood. Biol. Trace Element Res. 28:223-231.
    • (1991) Biol. Trace Element Res. , vol.28 , pp. 223-231
    • Jaffe, E.K.1    Bagla, S.2    Michini, P.A.3
  • 19
    • 0002132016 scopus 로고
    • The biosynthesis of 5-aminolevulinic acid and its transformation into coproporphyrinogen in animals and bacteria
    • H. A. Dailey (ed.), McGraw-Hill Publishing Co., New York, N.Y.
    • Jordan, P. M. 1990. The biosynthesis of 5-aminolevulinic acid and its transformation into coproporphyrinogen in animals and bacteria, p. 55-121. In H. A. Dailey (ed.), Biosynthesis of heme and chlorophylls. McGraw-Hill Publishing Co., New York, N.Y.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 55-121
    • Jordan, P.M.1
  • 20
    • 0031053298 scopus 로고    scopus 로고
    • Identification of the lrp gene in Bradyrhizobium japonicum and its role in regulation of δ-aminolevulinic acid uptake
    • King, N. D., and M. R. O'Brian. 1997. Identification of the lrp gene in Bradyrhizobium japonicum and its role in regulation of δ-aminolevulinic acid uptake. J. Bacteriol. 179:1828-1831.
    • (1997) J. Bacteriol. , vol.179 , pp. 1828-1831
    • King, N.D.1    O'Brian, M.R.2
  • 22
    • 0028854449 scopus 로고
    • The rhizobial hemA gene is required for symbiosis in species with deficient δ-aminolevulinic acid uptake activity
    • McGinnis, S. D., and M. R. O'Brian. 1995. The rhizobial hemA gene is required for symbiosis in species with deficient δ-aminolevulinic acid uptake activity. Plant Physiol. 108:1547-1552.
    • (1995) Plant Physiol. , vol.108 , pp. 1547-1552
    • McGinnis, S.D.1    O'Brian, M.R.2
  • 24
    • 0029863747 scopus 로고    scopus 로고
    • Heme synthesis in the rhizobium-legume symbiosis: A palette for bacterial and eukaryotic pigments
    • O'Brian, M. R. 1996. Heme synthesis in the rhizobium-legume symbiosis: a palette for bacterial and eukaryotic pigments. J. Bacteriol. 178:2471-2478.
    • (1996) J. Bacteriol. , vol.178 , pp. 2471-2478
    • O'Brian, M.R.1
  • 25
    • 0028194833 scopus 로고
    • Effect of iron availability on expression of the Bradyrhizobium japonicum hemA gene
    • Page, K. M., E. L. Connolly, and M. L. Guerinot. 1994. Effect of iron availability on expression of the Bradyrhizobium japonicum hemA gene. J. Bacteriol. 176:1535-1538.
    • (1994) J. Bacteriol. , vol.176 , pp. 1535-1538
    • Page, K.M.1    Connolly, E.L.2    Guerinot, M.L.3
  • 26
    • 0029020772 scopus 로고
    • Oxygen control of the Bradyrhizobium japonicum hemA gene
    • Page, K. M., and M. L. Guerinot. 1995. Oxygen control of the Bradyrhizobium japonicum hemA gene. J. Bacteriol. 177:3979-3984.
    • (1995) J. Bacteriol. , vol.177 , pp. 3979-3984
    • Page, K.M.1    Guerinot, M.L.2
  • 27
    • 0000892106 scopus 로고
    • Evidence for an inter-organismic heme biosynthetic pathway in symbiotic soybean root nodules
    • Sangwan, I., and M. R. O'Brian. 1991. Evidence for an inter-organismic heme biosynthetic pathway in symbiotic soybean root nodules. Science 251: 1220-1222.
    • (1991) Science , vol.251 , pp. 1220-1222
    • Sangwan, I.1    O'Brian, M.R.2
  • 28
    • 0029970569 scopus 로고    scopus 로고
    • Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor
    • Sellers, V. M., M. K. Johnson, and H. A. Dailey. 1996. Function of the [2Fe-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor. Biochemistry 35:2699-2704.
    • (1996) Biochemistry , vol.35 , pp. 2699-2704
    • Sellers, V.M.1    Johnson, M.K.2    Dailey, H.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.