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Volumn 255, Issue 4, 1997, Pages 376-381

Effects of starvation for heme on the synthesis of porphyrins in Escherichia coli

Author keywords

Glutamyl tRNA reductase; Heme; Porphyrin; Stringent response

Indexed keywords

AMINOLEVULINIC ACID; HEME; HEMIN; PORPHYRIN;

EID: 0030929420     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050509     Document Type: Article
Times cited : (14)

References (35)
  • 1
    • 0024371112 scopus 로고
    • Identification of the enzymatic basis for δ-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli
    • Avissar YJ, Beale SI (1989a) Identification of the enzymatic basis for δ-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli. J Bacteriol 171:2919-2924
    • (1989) J Bacteriol , vol.171 , pp. 2919-2924
    • Avissar, Y.J.1    Beale, S.I.2
  • 2
    • 0024369147 scopus 로고
    • Distribution of δ-aminolevulinic acid biosynthetic pathways among phototrophic bacterial groups
    • Avissar YJ, and Beale SI (1989b) 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    Beale, S.I.2
  • 3
    • 0011865764 scopus 로고
    • Biosynthesis of δ-aminolevulinic acid from the intact carbon skeleton of glutamic acid in greening barley
    • Beale SI, Gough SP, Granick S (1975) Biosynthesis of δ-aminolevulinic acid from the intact carbon skeleton of glutamic acid in greening barley. Proc Natl Acad Sci USA 72:2719-2723
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2719-2723
    • Beale, S.I.1    Gough, S.P.2    Granick, S.3
  • 5
    • 0001247852 scopus 로고
    • Chlorophyll biosynthesis: Recent advances and areas of current interest
    • Castelfranco PA, Beale SI (1983) Chlorophyll biosynthesis: recent advances and areas of current interest. Annu Rev Plant Physiol 34:241-278
    • (1983) Annu Rev Plant Physiol , vol.34 , pp. 241-278
    • Castelfranco, P.A.1    Beale, S.I.2
  • 6
    • 0030067385 scopus 로고    scopus 로고
    • Transcription of the glutamyl-tRNA reductase (hemA) gene in Salmonella typhimurium and Escherichia coli: Role of the hemA P1 promoter and the arcA gene product
    • Choi P, Wang L, Archer CD, Elliott T (1996) Transcription of the glutamyl-tRNA reductase (hemA) gene in Salmonella typhimurium and Escherichia coli: role of the hemA P1 promoter and the arcA gene product. J Bacteriol 178:638-646
    • (1996) J Bacteriol , vol.178 , pp. 638-646
    • Choi, P.1    Wang, L.2    Archer, C.D.3    Elliott, T.4
  • 7
    • 0015542618 scopus 로고
    • Porphyrin-accumulating mutants of Escherichia coli
    • Cox R, Charles HP (1973) Porphyrin-accumulating mutants of Escherichia coli. J Bacteriol 113:122-132
    • (1973) J Bacteriol , vol.113 , pp. 122-132
    • Cox, R.1    Charles, H.P.2
  • 8
    • 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, Gunsalus RP (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
  • 9
    • 0022971553 scopus 로고
    • Ribonuclease-sensitive δ-aminolevulinic acid formation from glutamate in cell extracts of Methanobacterium thermoautotrophicum
    • Friedmann HC, Thauer RK (1986) Ribonuclease-sensitive δ-aminolevulinic acid formation from glutamate in cell extracts of Methanobacterium thermoautotrophicum. FEBS Lett 207:84-88
    • (1986) FEBS Lett , vol.207 , pp. 84-88
    • Friedmann, H.C.1    Thauer, R.K.2
  • 10
    • 0021135330 scopus 로고
    • δ-Aminolevulinic acid-synthesizing enzymes need an RNA moiety for activity
    • Huang DD, Wang XY, Gough SP, Kannangara GC (1984) δ-Aminolevulinic acid-synthesizing enzymes need an RNA moiety for activity. Science 225:1482-1484
    • (1984) Science , vol.225 , pp. 1482-1484
    • Huang, D.D.1    Wang, X.Y.2    Gough, S.P.3    Kannangara, G.C.4
  • 11
    • 0002132016 scopus 로고
    • Biosynthesis of 5-aminolevulinic acid and its transformation into coproporphyrinogen in animals and bacteria
    • Dailey HA (ed) McGraw-Hill, New York
    • Jordan PM (1990) Biosynthesis of 5-aminolevulinic acid and its transformation into coproporphyrinogen in animals and bacteria. In: Dailey HA (ed) Biosynthesis of Heme and Chlorophylls. McGraw-Hill, New York, pp 55-212
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 55-212
    • Jordan, P.M.1
  • 12
    • 0022559019 scopus 로고
    • Purification of porphobilinogen synthetase from bovine liver
    • Jordan PM, Seehra JS (1986) Purification of porphobilinogen synthetase from bovine liver. Methods Enzymol 123:427-434
    • (1986) Methods Enzymol , vol.123 , pp. 427-434
    • Jordan, P.M.1    Seehra, J.S.2
  • 14
    • 0024471582 scopus 로고
    • Cloning and structure of the hemA gene of Escherichia coli K-12
    • Li JM, Russell CS, Cosloy SD (1989a) Cloning and structure of the hemA gene of Escherichia coli K-12. Gene 82:209-217
    • (1989) Gene , vol.82 , pp. 209-217
    • Li, J.M.1    Russell, C.S.2    Cosloy, S.D.3
  • 16
    • 0023656125 scopus 로고
    • Enzymatic conversion of glutamate to δ-aminolevulinic acid in soluble extracts of Euglena gracilis
    • Mayer SM, Beale SI, Weinstein JD (1987) Enzymatic conversion of glutamate to δ-aminolevulinic acid in soluble extracts of Euglena gracilis. J Biol Chem 262:12541-12549
    • (1987) J Biol Chem , vol.262 , pp. 12541-12549
    • Mayer, S.M.1    Beale, S.I.2    Weinstein, J.D.3
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Miller JF (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • (1972) Experiments in Molecular Genetics
    • Miller, J.F.1
  • 18
    • 0019312356 scopus 로고
    • The effect of alcohols on guanosine 5′-diphosphate-3′-diphosphate metabolism in stringent and relaxed Escherichia coli
    • Mitchell JJ, Lucas-Lenard JM (1980) The effect of alcohols on guanosine 5′-diphosphate-3′-diphosphate metabolism in stringent and relaxed Escherichia coli. J Biol Chem 255:6307-6313
    • (1980) J Biol Chem , vol.255 , pp. 6307-6313
    • Mitchell, J.J.1    Lucas-Lenard, J.M.2
  • 19
    • 0025804026 scopus 로고
    • Isolation and characterization of visible light-sensitive mutants of Escherichia coli K-12
    • Miyamoto K, Nakahigashi K, Nishimura K, Inokuchi H (1991) Isolation and characterization of visible light-sensitive mutants of Escherichia coli K-12. J Mol Biol 219:393-398
    • (1991) J Mol Biol , vol.219 , pp. 393-398
    • Miyamoto, K.1    Nakahigashi, K.2    Nishimura, K.3    Inokuchi, H.4
  • 20
    • 0026760863 scopus 로고
    • Accumulation of protoporphyrin IX in light-sensitive mutants of Escherichia coli
    • Miyamoto K, Nishimura K, Masuda T, Tuji H, Inokuchi H (1992) Accumulation of protoporphyrin IX in light-sensitive mutants of Escherichia coli. FEBS Lett 310:246-248
    • (1992) FEBS Lett , vol.310 , pp. 246-248
    • Miyamoto, K.1    Nishimura, K.2    Masuda, T.3    Tuji, H.4    Inokuchi, H.5
  • 21
    • 0025833809 scopus 로고
    • Photosensitivity of a protoporphyrin-accumulating, light-sensitive mutant (visA) of Escherichia coli K-12
    • Nakahigashi K, Nishimura K, Miyamoto K, Inokuchi H (1991) Photosensitivity of a protoporphyrin-accumulating, light-sensitive mutant (visA) of Escherichia coli K-12. Proc Natl Acad Sci USA 88:10520-10524
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10520-10524
    • Nakahigashi, K.1    Nishimura, K.2    Miyamoto, K.3    Inokuchi, H.4
  • 22
    • 0028789214 scopus 로고
    • Partial inhibition of protein synthesis accelerates the synthesis of porphyrin in heme-deficient mutants of Escherichia coli
    • Nakayashiki T, Nishimura K, Tanaka R, Inokuchi H (1995) Partial inhibition of protein synthesis accelerates the synthesis of porphyrin in heme-deficient mutants of Escherichia coli. Mol Gen Genet 249:139-146
    • (1995) Mol Gen Genet , vol.249 , pp. 139-146
    • Nakayashiki, T.1    Nishimura, K.2    Tanaka, R.3    Inokuchi, H.4
  • 23
    • 0027525607 scopus 로고
    • Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12
    • Nishimura K, Nakayashiki T, Inokuchi H (1993) Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12. Gene 133:109-113
    • (1993) Gene , vol.133 , pp. 109-113
    • Nishimura, K.1    Nakayashiki, T.2    Inokuchi, H.3
  • 24
    • 0025134999 scopus 로고
    • Glu gene provides tRNA for protein and chlorophyll biosynthesis
    • Glu gene provides tRNA for protein and chlorophyll biosynthesis. J Bacteriol 172:6363-6371
    • (1990) J Bacteriol , vol.172 , pp. 6363-6371
    • O'Neil, G.P.1    Söll, D.2
  • 26
    • 0024454015 scopus 로고
    • δ-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA
    • O'Neil GP, Chen MW, Söll D (1989) δ-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiol Lett 60:255-260
    • (1989) FEMS Microbiol Lett , vol.60 , pp. 255-260
    • O'Neil, G.P.1    Chen, M.W.2    Söll, D.3
  • 27
    • 0024707099 scopus 로고
    • Transformation of glutamate to δ-aminolevulinic acid by soluble extracts of Chlorobium vibrioforme
    • Rieble S, Beale SI (1988) Transformation of glutamate to δ-aminolevulinic acid by soluble extracts of Chlorobium vibrioforme. J Bacteriol 171:3782-3787
    • (1988) J Bacteriol , vol.171 , pp. 3782-3787
    • Rieble, S.1    Beale, S.I.2
  • 29
    • 0014137191 scopus 로고
    • Locus determining normal colony formation on the chromosome of Escherichia coli K-12
    • Sasarman A, Horodniceanu T (1967) Locus determining normal colony formation on the chromosome of Escherichia coli K-12. J Bacteriol 94:1268-1269
    • (1967) J Bacteriol , vol.94 , pp. 1268-1269
    • Sasarman, A.1    Horodniceanu, T.2
  • 30
    • 0000441055 scopus 로고
    • Biosynthesis of protoheme and heme precursors from glutamate in maize
    • Schneegurt MA, Beale SI (1986) Biosynthesis of protoheme and heme precursors from glutamate in maize. Plant Physiol 81:965-971
    • (1986) Plant Physiol , vol.81 , pp. 965-971
    • Schneegurt, M.A.1    Beale, S.I.2
  • 31
    • 0001571980 scopus 로고
    • 5-Aminolevulinic acid, its role in the biosynthesis of porphyrin and purines
    • Shemin D, Russell CS (1953) 5-Aminolevulinic acid, its role in the biosynthesis of porphyrin and purines. J Amer Chem Soc 75:4873-4875
    • (1953) J Amer Chem Soc , vol.75 , pp. 4873-4875
    • Shemin, D.1    Russell, C.S.2
  • 32
    • 0022426164 scopus 로고
    • RNA is required for enzymatic conversion of glutamate to δ-aminolevulinate by extracts of Chlorella vulgaris
    • Weinstein JD, Beale SI (1985a) RNA is required for enzymatic conversion of glutamate to δ-aminolevulinate by extracts of Chlorella vulgaris. Arch Biochem Biophys 239:87-93
    • (1985) Arch Biochem Biophys , vol.239 , pp. 87-93
    • Weinstein, J.D.1    Beale, S.I.2
  • 33
    • 0022032968 scopus 로고
    • Enzymatic conversion of glutamate to δ-aminolevulinate in soluble extracts of the unicellular alga Chlorella vulgaris
    • Weinstein JD, Beule SI (1985b) Enzymatic conversion of glutamate to δ-aminolevulinate in soluble extracts of the unicellular alga Chlorella vulgaris. Arch Biochem Biophys 237:454-464
    • (1985) Arch Biochem Biophys , vol.237 , pp. 454-464
    • Weinstein, J.D.1    Beule, S.I.2
  • 34
    • 2442544796 scopus 로고
    • Stimulation of δ-aminolevulinic acid formation in algal extracts by heterologous RNA
    • Weinstein JD, Mayer SM, Beale SI (1986) Stimulation of δ-aminolevulinic acid formation in algal extracts by heterologous RNA. Plant Physiol 82:1096-1101
    • (1986) Plant Physiol , vol.82 , pp. 1096-1101
    • Weinstein, J.D.1    Mayer, S.M.2    Beale, S.I.3
  • 35
    • 0028890255 scopus 로고
    • Regulation of heme biosynthesis in Escherichia coli
    • Woodard SI, Dailey HA (1995) Regulation of heme biosynthesis in Escherichia coli. Arch Biochem Biophys 316:110-115
    • (1995) Arch Biochem Biophys , vol.316 , pp. 110-115
    • Woodard, S.I.1    Dailey, H.A.2


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