메뉴 건너뛰기




Volumn 178, Issue 9, 1996, Pages 2471-2478

Heme synthesis in the rhizobium-legume symbiosis: A palette for bacterial and eukaryotic pigments

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; CYTOCHROME C; HEME; HEMOGLOBIN; HYDROLYASE;

EID: 0029863747     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.9.2471-2478.1996     Document Type: Short Survey
Times cited : (43)

References (95)
  • 1
    • 9244238460 scopus 로고
    • Ph.D thesis. Australian National University
    • Andersson, C. 1995. Ph.D thesis. Australian National University
    • (1995)
    • Andersson, C.1
  • 2
    • 0026573942 scopus 로고
    • Characterization of a fixLJ-regulated Bradyrhizobium japonicum gene sharing similarity with the Escherichia coli fnr and Rhizobium meliloti ftxK genes
    • Anthamatten, D., B. Scherb, and H. Hennecke. 1992 Characterization of a fixLJ-regulated Bradyrhizobium japonicum gene sharing similarity with the Escherichia coli fnr and Rhizobium meliloti ftxK genes. J. Bacteriol. 174: 2111-2120.
    • (1992) J. Bacteriol. , vol.174 , pp. 2111-2120
    • Anthamatten, D.1    Scherb, B.2    Hennecke, H.3
  • 3
    • 0000870242 scopus 로고
    • Leghemoglobin and Rhizobium respiration
    • Appleby, C. A. 1984. Leghemoglobin and Rhizobium respiration Annu. Rev Plant Physiol. 35:443-478
    • (1984) Annu. Rev Plant Physiol. , vol.35 , pp. 443-478
    • Appleby, C.A.1
  • 4
    • 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. 76:365-398.
    • (1992) Sci. Prog. , vol.76 , pp. 365-398
    • Appleby, C.A.1
  • 5
    • 0000805468 scopus 로고
    • Hemoglobin in a nonleguminous plant, Parasponia: Possible genetic origin and function in nitrogen fixation
    • Appleby, C. A., J. D. Tjepkema, and M. J. Trinick. 1983. Hemoglobin in a nonleguminous plant, Parasponia: possible genetic origin and function in nitrogen fixation. Science 220:951-953.
    • (1983) Science , vol.220 , pp. 951-953
    • Appleby, C.A.1    Tjepkema, J.D.2    Trinick, M.J.3
  • 6
    • 0018079850 scopus 로고
    • Stimulation of tetrapyrrole formation in Rhizobium japonicum by restricted aeration
    • Avissar, Y. J., and K. D. Nadler. 1978. Stimulation of tetrapyrrole formation in Rhizobium japonicum by restricted aeration. J. Bacteriol. 135:782-789.
    • (1978) J. Bacteriol. , vol.135 , pp. 782-789
    • Avissar, Y.J.1    Nadler, K.D.2
  • 7
    • 0024369147 scopus 로고
    • Distribution of δ-aminolevulinic acid biosynthetic pathways among phototrophic bacterial groups
    • Avissar, Y. J., J. G. Ormerod, and S. I. Beale. 1989. Distribution of δ-aminolevulinic acid biosynthetic pathways among phototrophic bacterial groups. Arch. Microbiol. 151:513-519.
    • (1989) Arch. Microbiol. , vol.151 , pp. 513-519
    • Avissar, Y.J.1    Ormerod, J.G.2    Beale, S.I.3
  • 8
    • 0024445091 scopus 로고
    • fixK, a gene homologous with fnr and crp from Escherichia coli, regulates nitrogen fixation genes both positively and negatively in Rhizobium meliloti
    • Batut, J., M.-L. Daveran-Mingon, M. David, J. Jacobs, A. M. Garnerone, and D. Kahn. 1989. fixK, a gene homologous with fnr and crp from Escherichia coli, regulates nitrogen fixation genes both positively and negatively in Rhizobium meliloti. EMBO J. 8:1279-1286.
    • (1989) EMBO J. , vol.8 , pp. 1279-1286
    • Batut, J.1    Daveran-Mingon, M.-L.2    David, M.3    Jacobs, J.4    Garnerone, A.M.5    Kahn, D.6
  • 9
    • 0002383191 scopus 로고
    • Tetrapyrrole metabolism in photosynthetic organisms
    • H. A. Dailcy (ed.). McGraw-Hill Publishing Co., New York
    • Beale, S. I., and J. D. Weinstein. 1990. Tetrapyrrole metabolism in photosynthetic organisms, p. 287-391 In H. A. Dailcy (ed.). Biosynthesis of heme and chlorophylls. McGraw-Hill Publishing Co., New York.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 287-391
    • Beale, S.I.1    Weinstein, J.D.2
  • 10
    • 0001575727 scopus 로고
    • The circadian oscillator coordinates the synthesis of apoproteins and their pigments during chloroplast development
    • Beator, J., and K. Kloppstech. 1993. The circadian oscillator coordinates the synthesis of apoproteins and their pigments during chloroplast development. Plant Physiol. 103:191-196
    • (1993) Plant Physiol. , vol.103 , pp. 191-196
    • Beator, J.1    Kloppstech, K.2
  • 11
  • 12
    • 0026014150 scopus 로고
    • Aminolevulinic acid in pea (Pisum sativum L.). Identification of an unusual metal binding domain in the plant enzyme
    • Boese, Q. F., A. J. Spano, J. Li, and M. P. Timko. 1991. Aminolevulinic acid in pea (Pisum sativum L.). Identification of an unusual metal binding domain in the plant enzyme. J Biol. Chem. 266:17060-17066.
    • (1991) J Biol. Chem. , vol.266 , pp. 17060-17066
    • Boese, Q.F.1    Spano, A.J.2    Li, J.3    Timko, M.P.4
  • 15
    • 0027432041 scopus 로고
    • Bradyrhizobium japonicum δ-amino-levulinic 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-amino-levulinic 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
  • 16
    • 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
  • 17
    • 0025105632 scopus 로고
    • An Fnr-like protein encoded in Rhizobium leguminosarum biovar viciae shows structural and functional homology to Rhizobium meliloti FixK
    • Colonna-Romano, S., W. Arnold, A. Schluter, P. Boistard, A. Puhler, and U. B. Priefer. 1990. An Fnr-like protein encoded in Rhizobium leguminosarum biovar viciae shows structural and functional homology to Rhizobium meliloti FixK. Mol. Gen. Genet. 223:138-147.
    • (1990) Mol. Gen. Genet. , vol.223 , pp. 138-147
    • Colonna-Romano, S.1    Arnold, W.2    Schluter, A.3    Boistard, P.4    Puhler, A.5    Priefer, U.B.6
  • 18
    • 0026566904 scopus 로고
    • A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence analysis of the gene
    • Coomber, S. A., R. M. Jones, P. M. Jordan, and C. N. Hunter. 1992. A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence analysis of the gene. Mol. Microbiol. 6:3156-3169.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3156-3169
    • Coomber, S.A.1    Jones, R.M.2    Jordan, P.M.3    Hunter, C.N.4
  • 19
    • 0014696465 scopus 로고
    • The site of heme synthesis in soybean root nodules
    • Cutting, J. A., and H. M. Schulman. 1969. The site of heme synthesis in soybean root nodules Biochim. Biophys. Acta 192:486-493
    • (1969) Biochim. Biophys. Acta , vol.192 , pp. 486-493
    • Cutting, J.A.1    Schulman, H.M.2
  • 21
    • 0027979040 scopus 로고
    • Effect of heme and oxygen availability on hemA gene expression in Escherichia coli: Role of the fnr, arcA, and himA gene products
    • Darie, S., and R. P. Gunsalus. 1994. Effect of heme and oxygen availability on hemA gene expression in Escherichia coli: role of the fnr, arcA, and himA gene products. J. Bacteriol. 176:5270-5276.
    • (1994) J. Bacteriol. , vol.176 , pp. 5270-5276
    • Darie, S.1    Gunsalus, R.P.2
  • 22
    • 0346566392 scopus 로고
    • Molecular genetics of nitrogen fixation by Azorhizobium caulinodans ORS571, the diazotrophic stem nodulating symbiont of Sesbania rostrata
    • F Bothe, J. de Bruijn, and W. E. Newton (ed.), Gustav Fischer, New York
    • de Bruijn, F. J., K. Pawlowski, P. Ratet, U. Hilgert, C. H. Wong, M. Schneider, H. Meyer Z. A., and J. Schell. 1988. Molecular genetics of nitrogen fixation by Azorhizobium caulinodans ORS571, the diazotrophic stem nodulating symbiont of Sesbania rostrata, p. 351-355 In F Bothe, J. de Bruijn, and W. E. Newton (ed.), Nitrogen fixation: hundred years after. Gustav Fischer, New York.
    • (1988) Nitrogen Fixation: Hundred Years after , pp. 351-355
    • De Bruijn, F.J.1    Pawlowski, K.2    Ratet, P.3    Hilgert, U.4    Wong, C.H.5    Schneider, M.6    Meyer Z. A., H.7    Schell, J.8
  • 23
    • 0029088169 scopus 로고
    • Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum
    • Delgado, M.-J., K. H. Yeoman, G. Wu, C. Vargas, A. E. Davies, R. K. Poole, A. W. B. Johnston, and J. A. Downie. 1995. Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum. J. Bacteriol. 177:4927-4934.
    • (1995) J. Bacteriol. , vol.177 , pp. 4927-4934
    • Delgado, M.-J.1    Yeoman, K.H.2    Wu, G.3    Vargas, C.4    Davies, A.E.5    Poole, R.K.6    Johnston, A.W.B.7    Downie, J.A.8
  • 24
    • 0027519716 scopus 로고
    • Lipo-oligosaccharide nudulation factors: A new class of signaling molecules mediating recognition and morphogenesis
    • Denarie, J., and J. Cullimore. 1993. Lipo-oligosaccharide nudulation factors: A new class of signaling molecules mediating recognition and morphogenesis. Cell 74:951-954
    • (1993) Cell , vol.74 , pp. 951-954
    • Denarie, J.1    Cullimore, J.2
  • 25
    • 0025719167 scopus 로고
    • Nodules elicited by Rhizobium meliloti heme mutants are arrested at an early stage in development
    • Dickstein, R., D. C. Scheirer, W. H. Fowle, and F. M. Ausubel. 1991. Nodules elicited by Rhizobium meliloti heme mutants are arrested at an early stage in development. Mol. Gen. Genet. 230:423-432
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 423-432
    • Dickstein, R.1    Scheirer, D.C.2    Fowle, W.H.3    Ausubel, F.M.4
  • 26
    • 7844244034 scopus 로고
    • Ferrochelatase activities and heme contents in purified mitochondria from soybean root nodules
    • Dimitrijevic, L., A. Puppo, J.-C. Trinchant, and J. Rigaud. 1989. Ferrochelatase activities and heme contents in purified mitochondria from soybean root nodules. J Plant Physiol. 134:642-644.
    • (1989) J Plant Physiol. , vol.134 , pp. 642-644
    • Dimitrijevic, L.1    Puppo, A.2    Trinchant, J.-C.3    Rigaud, J.4
  • 27
    • 0026766340 scopus 로고
    • Rhizobium-plant signal exchange
    • Fisher, R. F., and S. R. Long. 1992. Rhizobium-plant signal exchange Nature (London) 357:655-660.
    • (1992) Nature (London) , vol.357 , pp. 655-660
    • Fisher, R.F.1    Long, S.R.2
  • 28
    • 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
  • 29
    • 0027176620 scopus 로고
    • Analysis of the Bradyrhizobium japonicum hemH gene and expression in Escherichia coli
    • Frustaci, J. M., and M. R. O'Brian. 1993. Analysis of the Bradyrhizobium japonicum hemH gene and expression in Escherichia coli. Appl. Env. Microbiol. 59:2347-2351
    • (1993) Appl. Env. Microbiol. , vol.59 , pp. 2347-2351
    • Frustaci, J.M.1    O'Brian, M.R.2
  • 30
    • 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
  • 31
    • 0028965093 scopus 로고
    • Gsa1 is a universal tetrapyrrole synthesis gene in soybean and is resulated by a GAGA element
    • Frustaci, J. M., I. Sangwan, and M. R. O'Brian. 1995. Gsa1 is a universal tetrapyrrole synthesis gene in soybean and is resulated by a GAGA element J. Biol. Chem. 270:7387-7393.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7387-7393
    • Frustaci, J.M.1    Sangwan, I.2    O'Brian, M.R.3
  • 32
    • 0026564374 scopus 로고
    • A putative coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon
    • Gibson, C. D., P. McGlynn, M. Chaudhri, and C. N. Hunter. 1992. A putative coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon. Mol. Microbiol. 6: 3171-3186.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3171-3186
    • Gibson, C.D.1    McGlynn, P.2    Chaudhri, M.3    Hunter, C.N.4
  • 33
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez, M. A., G. S. Ditta, and D. R. Helinski. 1991. A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature (London) 350:170-172.
    • (1991) Nature (London) , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 34
    • 0015166919 scopus 로고
    • 14C]-δ-ammolevulinic acid in laboratory grown and root nodule Rhizobium lupini
    • 14C]-δ-ammolevulinic acid in laboratory grown and root nodule Rhizobium lupini. J Gen. Microbrol. 69:385-390.
    • (1971) J Gen. Microbrol. , vol.69 , pp. 385-390
    • Godfrey, C.A.1    Dilworth, M.J.2
  • 35
    • 0024273450 scopus 로고
    • Regulation of the erythropoietin gene: Evidence that the oxygen sensor is a heme protein
    • Goldberg, M. A., S. P. Dunning, and H. F. Bunn. 1988. Regulation of the erythropoietin gene: evidence that the oxygen sensor is a heme protein. Science 242:1412-1415.
    • (1988) Science , vol.242 , pp. 1412-1415
    • Goldberg, M.A.1    Dunning, S.P.2    Bunn, H.F.3
  • 36
    • 0022516509 scopus 로고
    • Bacterial δ-aminolevulinic acid synthase activity is not essential for leghemogiobin 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 leghemogiobin 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
  • 37
    • 0026755591 scopus 로고
    • Δ-Aminolevulinate uptake by Rhizobium bacteroids and its limitation by the peribacteroid membrane in legume root nodules
    • Herrada, G., A. Puppo, and J. Rigaud. 1992. Δ-Aminolevulinate uptake by Rhizobium bacteroids and its limitation by the peribacteroid membrane in legume root nodules. Biochem. Biophys. Res. Commun. 184:1324-1330.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1324-1330
    • Herrada, G.1    Puppo, A.2    Rigaud, J.3
  • 38
    • 0027947186 scopus 로고
    • The biosynthesis of bacterial and plastidic c-type cytochromes
    • Howe, G., and S. Merchant. 1994. The biosynthesis of bacterial and plastidic c-type cytochromes. Photosynth. Res. 40:147-165.
    • (1994) Photosynth. Res. , vol.40 , pp. 147-165
    • Howe, G.1    Merchant, S.2
  • 39
    • 0000353108 scopus 로고
    • Regulation of 5-aminolevulinic acid (ALA) synthesis in developing chloroplasts. III. Evidence for functional heterogeneity of the ALA pool
    • Huang, L., and P. A. Custelfranco. 1990. Regulation of 5-aminolevulinic acid (ALA) synthesis in developing chloroplasts. III. Evidence for functional heterogeneity of the ALA pool. Plant Physiol 92:172-178
    • (1990) Plant Physiol , vol.92 , pp. 172-178
    • Huang, L.1    Custelfranco, P.A.2
  • 40
    • 0028369994 scopus 로고
    • Light regulation of chlorophyll biosynthesis at the level of 5-ammolevulinate formation in Arabidopsis
    • Ilag, L. L., M. Kumar, and D. Söll. 1994. Light regulation of chlorophyll biosynthesis at the level of 5-ammolevulinate formation in Arabidopsis. Plant Cell 6:265-275.
    • (1994) Plant Cell , vol.6 , pp. 265-275
    • Ilag, L.L.1    Kumar, M.2    Söll, D.3
  • 42
    • 0025816348 scopus 로고
    • Two glutamyl-tRNA reductase activities in Eschenchia coli
    • Jahn, D., U. Michelsen, and D. Söll. 1991. Two glutamyl-tRNA reductase activities in Eschenchia coli J Biol Chem. 266:2542-2548.
    • (1991) J Biol Chem. , vol.266 , pp. 2542-2548
    • Jahn, D.1    Michelsen, U.2    Söll, D.3
  • 43
    • 0026686195 scopus 로고
    • Glutamyl-transfer RNA: A precursor of heme and chlorophyll biosynthesis
    • Jahn, D., E. Verkamp, and D. Söll. 1991. Glutamyl-transfer RNA: a precursor of heme and chlorophyll biosynthesis. Trends Biochem. Sci. 17:215-218.
    • (1991) Trends Biochem. Sci. , vol.17 , pp. 215-218
    • Jahn, D.1    Verkamp, E.2    Söll, D.3
  • 44
    • 0028983450 scopus 로고
    • orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria
    • Jekabsons, W., and W. Schuster. 1995. orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria. Mol Gen Genet. 246:166-173.
    • (1995) Mol Gen Genet. , vol.246 , pp. 166-173
    • Jekabsons, W.1    Schuster, W.2
  • 45
    • 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
    • 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.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 55-121
    • Jordan, P.M.1
  • 46
    • 0028603602 scopus 로고
    • Highlights in haem biosynthesis
    • Jordan, P. M. 1994. Highlights in haem biosynthesis. Curr. Opin. Struc. Biol. 4:902-911.
    • (1994) Curr. Opin. Struc. Biol. , vol.4 , pp. 902-911
    • Jordan, P.M.1
  • 47
    • 0001017449 scopus 로고
    • Isolation of plastids of buds of cauliflower (Brassica oleracea L.)
    • Journet, E.-P. 1991. Isolation of plastids of buds of cauliflower (Brassica oleracea L.). Methods Enzymol 148:234-240.
    • (1991) Methods Enzymol , vol.148 , pp. 234-240
    • Journet, E.-P.1
  • 48
    • 0028410517 scopus 로고
    • Plant δ-aminolevulinic acid dehydratase. Expression in soybean root nodules and evidence for a bacterial lineage of the Alad gene
    • Kaczor, C. M., W. Smith, I. Sangwan, and M. R. O'Brian. 1994. Plant δ-aminolevulinic acid dehydratase. Expression in soybean root nodules and evidence for a bacterial lineage of the Alad gene. Plant Physiol. 104:1411-1417.
    • (1994) Plant Physiol. , vol.104 , pp. 1411-1417
    • Kaczor, C.M.1    Smith, W.2    Sangwan, I.3    O'Brian, M.R.4
  • 49
    • 0027332478 scopus 로고
    • 2-utilizing cytochrome c oxidase complex from Bradyrhizobium japonicum bacteroid membranes
    • 2-utilizing cytochrome c oxidase complex from Bradyrhizobium japonicum bacteroid membranes. Biochim. Biophys. Acta 1183:91-104.
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 91-104
    • Keefe, R.G.1    Maier, R.J.2
  • 50
    • 0020622404 scopus 로고
    • Protoporphyrin formation in Rhizobium japonicum
    • Keithly, J. H., and K. D. Nadler. 1983. Protoporphyrin formation in Rhizobium japonicum. J. Bacteriol. 154:838-845.
    • (1983) J. Bacteriol. , vol.154 , pp. 838-845
    • Keithly, J.H.1    Nadler, K.D.2
  • 51
    • 0023504597 scopus 로고
    • Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression
    • Keng, T., and L. Guerente. 1987. Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression. Proc. Natl Acad. Sci. USA 84:9113-9117.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 9113-9117
    • Keng, T.1    Guerente, L.2
  • 52
    • 0028968401 scopus 로고
    • The cycHJKL genes of Rhizobium meliloti involved in cytochrome c biogenesis are required for "respiratory" nitrate reduction ex planta and for nitrogen fixation during symbiosis
    • Kereszt, A., K. Slaska-Kiss, P. Putnoky, Z. Banfalvi, and A. Kondorosi. 1995. The cycHJKL genes of Rhizobium meliloti involved in cytochrome c biogenesis are required for "respiratory" nitrate reduction ex planta and for nitrogen fixation during symbiosis Mol. Gen Genet. 247:39-47.
    • (1995) Mol. Gen Genet. , vol.247 , pp. 39-47
    • Kereszt, A.1    Slaska-Kiss, K.2    Putnoky, P.3    Banfalvi, Z.4    Kondorosi, A.5
  • 54
    • 0020479380 scopus 로고
    • Heme biosynthesis in Rhizobium Identification of a cloned gene coding for 6-aminolevulinic acid synthetase from Rhizobium meliloti
    • Leong, S. A., D. S. Ditta, and D. R. Helinski. 1982. Heme biosynthesis in Rhizobium Identification of a cloned gene coding for 6-aminolevulinic acid synthetase from Rhizobium meliloti. J. Biol Chem. 257:8724-8730.
    • (1982) J. Biol Chem. , vol.257 , pp. 8724-8730
    • Leong, S.A.1    Ditta, D.S.2    Helinski, D.R.3
  • 55
    • 0026688148 scopus 로고
    • Nitric oxide, a novel biologic messenger
    • Lowenstein, C. J., and S. H. Snyder. 1992. Nitric oxide, a novel biologic messenger. Cell 70:705-707.
    • (1992) Cell , vol.70 , pp. 705-707
    • Lowenstein, C.J.1    Snyder, S.H.2
  • 56
    • 0027335550 scopus 로고
    • n repeats and heat shock elements have distinct roles in chromatin structure and transcriptional activation of the Drosophila hsp26 gene
    • n repeats and heat shock elements have distinct roles in chromatin structure and transcriptional activation of the Drosophila hsp26 gene. Mol. Cell. Biol 13:2802-2814.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 2802-2814
    • Lu, Q.1    Wallrath, L.L.2    Granok, H.3    Elgin, S.C.R.4
  • 57
    • 0027673660 scopus 로고
    • A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules
    • Madsen, O., L. Sandal, N. N. Sandal, and K. A. Marcker. 1993. A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules Plant Mol. Biol. 23:35-43.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 35-43
    • Madsen, O.1    Sandal, L.2    Sandal, N.N.3    Marcker, K.A.4
  • 58
    • 0028854449 scopus 로고
    • The rhizobial hemA gene is required for symbiosis in species with deficient 8-ammolevulinic acid uptake activity
    • McGinnis, S. D., and M. R. O'Brian. 1995. The rhizobial hemA gene is required for symbiosis in species with deficient 8-ammolevulinic 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
  • 59
    • 1542712712 scopus 로고
    • Heme synthesis in soybean root nodules. On the role of bacteroid δ-aminolevulinic acid synthase and δ-aminolevulinic acid dehydratase in the synthesis of the heme of leghemoglobin
    • Nadler, K. D., and Y. J. Avissar. 1977. Heme synthesis in soybean root nodules. On the role of bacteroid δ-aminolevulinic acid synthase and δ-aminolevulinic acid dehydratase in the synthesis of the heme of leghemoglobin. Plant Physiol. 60:433-436.
    • (1977) Plant Physiol. , vol.60 , pp. 433-436
    • Nadler, K.D.1    Avissar, Y.J.2
  • 60
    • 0017329303 scopus 로고
    • Quaternary structure of δ-aminolevulinic acid synthase from Rhodopseudomonas sphaeroides
    • Nandi, D. L., and D. Shemin. 1977. Quaternary structure of δ-aminolevulinic acid synthase from Rhodopseudomonas sphaeroides J. Biol. Chem. 252:2278-2280.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2278-2280
    • Nandi, D.L.1    Shemin, D.2
  • 61
    • 0023497733 scopus 로고
    • Bacterial heme synthesis is required for expression of the leghemoglobin holoprotein but not the apoprotein in soybean root nodules
    • O'Brian, M. R., P. M. Kirshbom, and R. J. Maier. 1987. Bacterial heme synthesis is required for expression of the leghemoglobin holoprotein but not the apoprotein in soybean root nodules Proc. Natl Acad Sci USA 84: 8390-8393.
    • (1987) Proc. Natl Acad Sci USA , vol.84 , pp. 8390-8393
    • O'Brian, M.R.1    Kirshbom, P.M.2    Maier, R.J.3
  • 62
    • 0024981178 scopus 로고
    • Molecular aspects of the energetics of nitrogen fixation in Rhizobium-legume symbioses
    • O'Brian, M. R., and R. J. Maier. 1989. Molecular aspects of the energetics of nitrogen fixation in Rhizobium-legume symbioses. Biochim. Biophys. Acta 974:229-246.
    • (1989) Biochim. Biophys. Acta , vol.974 , pp. 229-246
    • O'Brian, M.R.1    Maier, R.J.2
  • 63
    • 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
  • 66
    • 0025987220 scopus 로고
    • In vitro reconstitution of protein transport into chloroplasts
    • Perry, S. E., H. Li, and K. Keegstra. 1991 In vitro reconstitution of protein transport into chloroplasts. Methods Cell Biol. 34:327-344
    • (1991) Methods Cell Biol. , vol.34 , pp. 327-344
    • Perry, S.E.1    Li, H.2    Keegstra, K.3
  • 67
    • 0027469984 scopus 로고
    • Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis
    • Preisig, O., D. Anthamatten, and H. Hennecke. 1993. Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis. Proc. Natl. Acad. Sci. USA 90:3309-3313.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3309-3313
    • Preisig, O.1    Anthamatten, D.2    Hennecke, H.3
  • 68
    • 0025823215 scopus 로고
    • Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes
    • Ramseier, T. M., H. V. Winteler, and H. Hennecke. 1991. Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes. J. Biol. Chem. 266:7793-7803.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7793-7803
    • Ramseier, T.M.1    Winteler, H.V.2    Hennecke, H.3
  • 69
    • 0025900778 scopus 로고
    • Purification of glutamyl-tRNA reductase from Synechocystis sp. PCC6803
    • Rieble, S., and S. I. Beale. 1991. Purification of glutamyl-tRNA reductase from Synechocystis sp. PCC6803. J. Biol. Chem. 266:9740-9745
    • (1991) J. Biol. Chem. , vol.266 , pp. 9740-9745
    • Rieble, S.1    Beale, S.I.2
  • 70
    • 0028964914 scopus 로고
    • The cycHJKL gene cluster plays an essential role in the biogenesis of c-type cytochromes in Bradyrhizobium japonicum
    • Ritz, D., L. Thony-Meyer, and H. Hennecke. 1995. The cycHJKL gene cluster plays an essential role in the biogenesis of c-type cytochromes in Bradyrhizobium japonicum Mol. Gen. Genet 247:27-38.
    • (1995) Mol. Gen. Genet , vol.247 , pp. 27-38
    • Ritz, D.1    Thony-Meyer, L.2    Hennecke, H.3
  • 71
    • 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
  • 72
    • 0344288143 scopus 로고
    • Characterization of δ-aminolevulinic acid formation in soybean root nodules
    • Sangwan, I., and M. R. O'Brian. 1992 Characterization of δ-aminolevulinic acid formation in soybean root nodules Plant Physiol. 98:1074-1079
    • (1992) Plant Physiol. , vol.98 , pp. 1074-1079
    • Sangwan, I.1    O'Brian, M.R.2
  • 73
    • 0027622612 scopus 로고
    • Expression of the soybean (Glycine max) glutamate 1-semialdehyde aminotransferase gene in symbiotic root nodules
    • Sangwan, I., and M. R. O'Brian. 1993. Expression of the soybean (Glycine max) glutamate 1-semialdehyde aminotransferase gene in symbiotic root nodules Plant Physiol 102:829-834
    • (1993) Plant Physiol , vol.102 , pp. 829-834
    • Sangwan, I.1    O'Brian, M.R.2
  • 74
    • 0028409698 scopus 로고
    • The highly edited orf206 in Oenothera mitochondria may encode a component of a heme transporter involved in cytochrome c biogenesis
    • Schuster, W. 1994. The highly edited orf206 in Oenothera mitochondria may encode a component of a heme transporter involved in cytochrome c biogenesis. Plant Mol Biol. 25:33-42.
    • (1994) Plant Mol Biol. , vol.25 , pp. 33-42
    • Schuster, W.1
  • 75
    • 0027155538 scopus 로고
    • A plant mitochondrial gene encodes a protein involved in cytochrome c biogenesis
    • Schuster, W., B. Combettes, K. Flieger, and A. Brennicke. 1993. A plant mitochondrial gene encodes a protein involved in cytochrome c biogenesis Mol. Gen. Genet. 239:49-57.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 49-57
    • Schuster, W.1    Combettes, B.2    Flieger, K.3    Brennicke, A.4
  • 76
    • 0027311993 scopus 로고
    • Regulating genes by packaging domains: Bits of heterochromatin in euchromatin?
    • Straffer, C. D., L. L. Wallrath, and S. C. R. Elgin. 1993. Regulating genes by packaging domains: bits of heterochromatin in euchromatin? Trends Genet. 9:35-37.
    • (1993) Trends Genet. , vol.9 , pp. 35-37
    • Straffer, C.D.1    Wallrath, L.L.2    Elgin, S.C.R.3
  • 77
    • 9244226269 scopus 로고
    • Isolation of amyloplasts from developing endosperm of Maize (Zea Mays L)
    • Shannon, J. C., E. Echeverria, and C. Boyer. 1987. Isolation of amyloplasts from developing endosperm of Maize (Zea Mays L) Methods Enzymol 148: 226-234.
    • (1987) Methods Enzymol , vol.148 , pp. 226-234
    • Shannon, J.C.1    Echeverria, E.2    Boyer, C.3
  • 78
    • 0024286451 scopus 로고
    • Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoo-pint) species
    • Smith, A. G. 1988. Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoo-pint) species. Biochem. J 249:423-428
    • (1988) Biochem. J , vol.249 , pp. 423-428
    • Smith, A.G.1
  • 79
    • 0027213464 scopus 로고
    • Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants
    • Smith, A. G., O. Marsh, and G. H. Elder. 1993. Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochem. J. 292:503-508.
    • (1993) Biochem. J. , vol.292 , pp. 503-508
    • Smith, A.G.1    Marsh, O.2    Elder, G.H.3
  • 80
    • 0027422982 scopus 로고
    • Isolation of cDNAs encoding the Drosphila GAGA transcription factor
    • Soeller, W. C., C. E. Oh, and T. B. Kornberg. 1993. Isolation of cDNAs encoding the Drosphila GAGA transcription factor. Mol. Cell. Biol 13: 7961-7970
    • (1993) Mol. Cell. Biol , vol.13 , pp. 7961-7970
    • Soeller, W.C.1    Oh, C.E.2    Kornberg, T.B.3
  • 82
    • 0001865912 scopus 로고
    • Cloning of hemA from Rluzobium sp. NGR234 and symbiotic phenotype of a gene-directed mutant in diverse legume genera
    • Stanley, J., D. N. Dowling, and W. J. Broughton. 1988. Cloning of hemA from Rluzobium sp. NGR234 and symbiotic phenotype of a gene-directed mutant in diverse legume genera. Mol. Gen. Genet. 215:32-37.
    • (1988) Mol. Gen. Genet. , vol.215 , pp. 32-37
    • Stanley, J.1    Dowling, D.N.2    Broughton, W.J.3
  • 83
    • 0000547350 scopus 로고
    • Carbohydrate, organic acid, and amino acid composition of bacteroids and cytosol from soybean nodules
    • Streeter, J. G. 1987 Carbohydrate, organic acid, and amino acid composition of bacteroids and cytosol from soybean nodules. Plant Physiol. 85:768-773
    • (1987) Plant Physiol. , vol.85 , pp. 768-773
    • Streeter, J.G.1
  • 84
    • 0028384684 scopus 로고
    • A cereal hemoglobin gene is expressed in seed and root tissues under anaerobic conditions
    • Taylor, E. R., X. Z. Nie, A. W. MacGregor, and R. D. Hill. 1994. A cereal hemoglobin gene is expressed in seed and root tissues under anaerobic conditions Plant Mol. Biol. 24:853-862.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 853-862
    • Taylor, E.R.1    Nie, X.Z.2    MacGregor, A.W.3    Hill, R.D.4
  • 86
    • 0028107485 scopus 로고
    • Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEMI3 mutant
    • Troup, B., M. Jahn, C. Hungerer, and D. Jahn. 1994. Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEMI3 mutant. J. Bacteriol. 176:673-680
    • (1994) J. Bacteriol. , vol.176 , pp. 673-680
    • Troup, B.1    Jahn, M.2    Hungerer, C.3    Jahn, D.4
  • 87
    • 0028055116 scopus 로고
    • ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor
    • Tsukiyama, T., P. B. Becker, and C. Wu. 1994. ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor. Nature (London) 367:525-532.
    • (1994) Nature (London) , vol.367 , pp. 525-532
    • Tsukiyama, T.1    Becker, P.B.2    Wu, C.3
  • 88
    • 0001946682 scopus 로고
    • A dicarboxylate transporter on the peribacteroid membrane of soybean nodules
    • Udvardi, M. K., G. D. Price, P. M. Gresshoff, and D. A. Day. 1988. A dicarboxylate transporter on the peribacteroid membrane of soybean nodules. FEBS Lett. 231:36-40.
    • (1988) FEBS Lett. , vol.231 , pp. 36-40
    • Udvardi, M.K.1    Price, G.D.2    Gresshoff, P.M.3    Day, D.A.4
  • 89
    • 0026640644 scopus 로고
    • Glutamyl-tRNA reductase from Eschenchia coli and Synechocystis 6803
    • Verkamp, E., M. Jahn, D. Jahn, A. M. Kumar, and D. Söll. 1992. Glutamyl-tRNA reductase from Eschenchia coli and Synechocystis 6803. J Biol. Chem. 267:8275-8280.
    • (1992) J Biol. Chem. , vol.267 , pp. 8275-8280
    • Verkamp, E.1    Jahn, M.2    Jahn, D.3    Kumar, A.M.4    Söll, D.5
  • 91
    • 0001069489 scopus 로고    scopus 로고
    • Isolation of intact chloroplasts: General principles and criteria of integrity
    • Walker, D. A., Z. G. Cerovic, and S. P. Robinson. Isolation of intact chloroplasts: general principles and criteria of integrity Methods Enzymol. 148: 145-157.
    • Methods Enzymol. , vol.148 , pp. 145-157
    • Walker, D.A.1    Cerovic, Z.G.2    Robinson, S.P.3
  • 92
    • 0026688997 scopus 로고
    • The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation
    • Xu, K., J. Delling, and T. Elliott. 1992 The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation. J. Bacteriol 174:3953-3963
    • (1992) J. Bacteriol , vol.174 , pp. 3953-3963
    • Xu, K.1    Delling, J.2    Elliott, T.3
  • 93
    • 0027205487 scopus 로고
    • An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium
    • Xu, K., and T. Elliott. 1993. An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. J. Bacteriol. 175:4990-4999.
    • (1993) J. Bacteriol. , vol.175 , pp. 4990-4999
    • Xu, K.1    Elliott, T.2
  • 94
    • 0028304529 scopus 로고
    • Cloning, DNA sequence, and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen independent coproporphyrinogen III oxidase
    • Xu, K., and T. Elliott. 1994 Cloning, DNA sequence, and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen independent coproporphyrinogen III oxidase. J. Bacteriol. 176:3196-3203.
    • (1994) J. Bacteriol. , vol.176 , pp. 3196-3203
    • Xu, K.1    Elliott, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.