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Volumn 173, Issue 1, 1999, Pages 175-182

Functional analysis of the hemK gene product involvement in protoporphyrinogen oxidase activity in yeast

Author keywords

Escherichia coli; Heme biosynthesis; HemG; HemK; Protoporphyrinogen oxidase; Yeast

Indexed keywords

METHYLTRANSFERASE; PROTOPORPHYRINOGEN OXIDASE;

EID: 0033040799     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00067-1     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 0017927528 scopus 로고
    • Hemes, chlorophylls, and related compounds: Biosynthesis and metabolic regulation
    • Granick, S. and Beale, S.I. (1978) Hemes, chlorophylls, and related compounds: biosynthesis and metabolic regulation. Adv. Enzymol. Relat. Areas Mol. Biol. 46, 33-203.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.46 , pp. 33-203
    • Granick, S.1    Beale, S.I.2
  • 2
    • 0004262533 scopus 로고    scopus 로고
    • Characteristics of protoporphyrinogen oxidase
    • Böger, P. and Wakabayashi, K., Eds., Springer Verlag, Berlin, Heidelberg
    • Camadro, J.M., Arnould, S., Le Guen, L., Santos, R., Matringe, M. and Mornet, R. (1999) Characteristics of protoporphyrinogen oxidase. In: Peroxizing Herbicides (Böger, P. and Wakabayashi, K., Eds.), pp. 245-277. Springer Verlag, Berlin, Heidelberg.
    • (1999) Peroxizing Herbicides , pp. 245-277
    • Camadro, J.M.1    Arnould, S.2    Le Guen, L.3    Santos, R.4    Matringe, M.5    Mornet, R.6
  • 3
    • 0011366330 scopus 로고
    • Induction of tetrapyrrole accumulation by diphenylether-type herbicides
    • Matringe, M. and Scalla, R. (1987) Induction of tetrapyrrole accumulation by diphenylether-type herbicides. 1987, British Crop Protection Conference-Weeds, Vol. 3, pp. 981-988.
    • (1987) 1987, British Crop Protection Conference-Weeds , vol.3 , pp. 981-988
    • Matringe, M.1    Scalla, R.2
  • 6
    • 0029185578 scopus 로고
    • Cloning and identification of the hemG gene encoding protoporphyrinogen oxidase (PPO) of Escherichia coli K-12
    • Nishimura, K., Nakayashiki, T. and Inokuchi, H. (1995) Cloning and identification of the hemG gene encoding protoporphyrinogen oxidase (PPO) of Escherichia coli K-12. DNA Res. 2, 1-8.
    • (1995) DNA Res. , vol.2 , pp. 1-8
    • Nishimura, K.1    Nakayashiki, T.2    Inokuchi, H.3
  • 7
    • 0027724541 scopus 로고
    • Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12
    • Sasarman, A., Letowski, J., Czaika, G., Ramirez, V., Nead, M.A., Jacobs, J.M. and Morais, R. (1993) Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12. Can. J. Microbiol. 39, 1155-1161.
    • (1993) Can. J. Microbiol. , vol.39 , pp. 1155-1161
    • Sasarman, A.1    Letowski, J.2    Czaika, G.3    Ramirez, V.4    Nead, M.A.5    Jacobs, J.M.6    Morais, R.7
  • 8
    • 0028797882 scopus 로고
    • Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli
    • Nakayashiki, T., Nishimura, K. and Inokuchi, H. (1995) Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli. Gene 153, 67-70.
    • (1995) Gene , vol.153 , pp. 67-70
    • Nakayashiki, T.1    Nishimura, K.2    Inokuchi, H.3
  • 9
    • 0019456518 scopus 로고
    • Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis
    • Urban-Grimal, D. and Labbe-Bois, R. (1981) Genetic and biochemical characterization of mutants of Saccharomyces cerevisiae blocked in six different steps of heme biosynthesis. Mol. Gen. Genet. 183, 85-92.
    • (1981) Mol. Gen. Genet. , vol.183 , pp. 85-92
    • Urban-Grimal, D.1    Labbe-Bois, R.2
  • 10
    • 0030012328 scopus 로고    scopus 로고
    • Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides
    • Camadro, J.M. and Labbe, P. (1996) Cloning and characterization of the yeast HEM14 gene coding for protoporphyrinogen oxidase, the molecular target of diphenyl ether-type herbicides. J. Biol. Chem. 271, 9120-9128.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9120-9128
    • Camadro, J.M.1    Labbe, P.2
  • 11
    • 0027969301 scopus 로고
    • Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX
    • Hansson, M. and Hederstedt, L. (1994) Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX. J. Bacteriol. 176, 5962-5970.
    • (1994) J. Bacteriol. , vol.176 , pp. 5962-5970
    • Hansson, M.1    Hederstedt, L.2
  • 12
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 13
    • 0027767502 scopus 로고
    • A series of yeast shuttle vectors for expression of cDNAs and other DNA sequences
    • Brunelli, J.P. and Pall, M.L. (1993) A series of yeast shuttle vectors for expression of cDNAs and other DNA sequences. Yeast 9, 1299-1308.
    • (1993) Yeast , vol.9 , pp. 1299-1308
    • Brunelli, J.P.1    Pall, M.L.2
  • 15
    • 0014644833 scopus 로고
    • Nouvelle technique de réalisation de spectres d'absorption à basse température
    • Labbe, P. and Chaix, P. (1969) Nouvelle technique de réalisation de spectres d'absorption à basse température. Bull. Soc. Chim. Biol. 51, 1642-1644.
    • (1969) Bull. Soc. Chim. Biol. , vol.51 , pp. 1642-1644
    • Labbe, P.1    Chaix, P.2
  • 16
    • 0028609358 scopus 로고
    • Purification and properties of protoporphyrinogen oxidase from the yeast Saccharomyces cerevisiae. Mitochondrial location and evidence for a precursor form of the protein
    • Camadro, J.M., Thome, F., Brouillet, N. and Labbe, P. (1994) Purification and properties of protoporphyrinogen oxidase from the yeast Saccharomyces cerevisiae. Mitochondrial location and evidence for a precursor form of the protein. J. Biol. Chem. 269, 32085-32091.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32085-32091
    • Camadro, J.M.1    Thome, F.2    Brouillet, N.3    Labbe, P.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the 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
  • 18
    • 0026002035 scopus 로고
    • The plasma membrane ferrireductase activity of Saccharomyces cerevisiae is partially controlled by cyclic AMP
    • Lesuisse, E., Horion, B., Labbe, P. and Hilger, F. (1991) The plasma membrane ferrireductase activity of Saccharomyces cerevisiae is partially controlled by cyclic AMP. Biochem. J. 280, 545-548.
    • (1991) Biochem. J. , vol.280 , pp. 545-548
    • Lesuisse, E.1    Horion, B.2    Labbe, P.3    Hilger, F.4
  • 19
    • 0023444132 scopus 로고
    • Iron uptake by the yeast Saccharomyces cerevisiae: Involvement of a reduction step
    • Lesuisse, E., Raguzzi, F. and Crichton, R.R. (1987) Iron uptake by the yeast Saccharomyces cerevisiae: involvement of a reduction step. J. Gen. Microbiol. 133, 3229-3336.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 3229-3336
    • Lesuisse, E.1    Raguzzi, F.2    Crichton, R.R.3
  • 20
    • 0020385409 scopus 로고
    • A new assay for protoporphyrinogen oxidase - Evidence for a total deficiency in that activity in a heme-less mutant of Saccharomyces cerevisiae
    • Camadro, J.M., Urban-Grimal, D. and Labbe, P. (1982) A new assay for protoporphyrinogen oxidase - evidence for a total deficiency in that activity in a heme-less mutant of Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 106, 724-730.
    • (1982) Biochem. Biophys. Res. Commun. , vol.106 , pp. 724-730
    • Camadro, J.M.1    Urban-Grimal, D.2    Labbe, P.3
  • 21
    • 0022246318 scopus 로고
    • Fluorometric assays for coproporphyrinogen oxidase and protoporphyrinogen oxidase
    • Labbe, P., Camadro, J.M. and Chambon, H. (1985) Fluorometric assays for coproporphyrinogen oxidase and protoporphyrinogen oxidase. Anal. Biochem. 149, 248-260.
    • (1985) Anal. Biochem. , vol.149 , pp. 248-260
    • Labbe, P.1    Camadro, J.M.2    Chambon, H.3
  • 22
    • 0016671103 scopus 로고
    • The enzymatic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae
    • Poulson, R. and Polglase, W.J. (1975) The enzymatic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae. J. Biol. Chem. 250, 1269-1274.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1269-1274
    • Poulson, R.1    Polglase, W.J.2
  • 23
    • 0028954222 scopus 로고
    • Ferri-reductase activity in Saccharomyces cerevisiae and other fungi: Colorimetric assays on agar plates
    • Lesuisse, E., Casteras-Simon, M. and Labbe, P. (1995) Ferri-reductase activity in Saccharomyces cerevisiae and other fungi: colorimetric assays on agar plates. Anal. Biochem. 226, 375-377.
    • (1995) Anal. Biochem. , vol.226 , pp. 375-377
    • Lesuisse, E.1    Casteras-Simon, M.2    Labbe, P.3
  • 24
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone, T., Blumenthal, R.M. and Cheng, X. (1995) Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253, 618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 25
    • 0018092069 scopus 로고
    • Comparative study of DNA methylation in three unicellular eukaryotes
    • Hattman, S., Kenny, C., Berger, L. and Pratt, K. (1978) Comparative study of DNA methylation in three unicellular eukaryotes. J. Bacteriol. 135, 1156-1157.
    • (1978) J. Bacteriol. , vol.135 , pp. 1156-1157
    • Hattman, S.1    Kenny, C.2    Berger, L.3    Pratt, K.4
  • 26
    • 8044258383 scopus 로고    scopus 로고
    • Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I
    • Blanc, V., Gil, P., Bamas-Jacques, N., Lorenzon, S., Zagorec, M., Schleuniger, J., Bisch, D., Blanche, F., Debussche, L., Crouzet, J. and Thibaut, D. (1997) Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-phenylalanine precursor of pristinamycin I. Mol. Microbiol. 23, 191-202.
    • (1997) Mol. Microbiol. , vol.23 , pp. 191-202
    • Blanc, V.1    Gil, P.2    Bamas-Jacques, N.3    Lorenzon, S.4    Zagorec, M.5    Schleuniger, J.6    Bisch, D.7    Blanche, F.8    Debussche, L.9    Crouzet, J.10    Thibaut, D.11
  • 27
    • 0030904143 scopus 로고    scopus 로고
    • Analysis of Xenopus dsRNA adenosine deaminase cDNAs reveals similarities to DNA methyltransferases
    • Hough, R.F. and Bass, B.L. (1997) Analysis of Xenopus dsRNA adenosine deaminase cDNAs reveals similarities to DNA methyltransferases. RNA 3, 356-370.
    • (1997) RNA , vol.3 , pp. 356-370
    • Hough, R.F.1    Bass, B.L.2
  • 28
    • 0030712151 scopus 로고    scopus 로고
    • Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase
    • Bokar, J.A., Shambaugh, M.E., Polayes, D., Matera, A.G. and Rottman, F.M. (1997) Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase. RNA 3, 1233-1247.
    • (1997) RNA , vol.3 , pp. 1233-1247
    • Bokar, J.A.1    Shambaugh, M.E.2    Polayes, D.3    Matera, A.G.4    Rottman, F.M.5
  • 29
    • 0027338134 scopus 로고
    • Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine
    • Cheng, X., Kumar, S., Posfai, J., Pflugrath, J.W. and Roberts, R.J. (1993) Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell 74, 299-307.
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Posfai, J.3    Pflugrath, J.W.4    Roberts, R.J.5
  • 30
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase M.TaqI in complex with the cofactor S-adenosylmethionine
    • Labahn, J., Granzin, J., Schluckebier, G., Robinson, D.P., Jack, W.E., Schildkraut, I. and Saenger, W. (1994) Three-dimensional structure of the adenine-specific DNA methyltransferase M.TaqI in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. USA 91, 10957-10961.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10957-10961
    • Labahn, J.1    Granzin, J.2    Schluckebier, G.3    Robinson, D.P.4    Jack, W.E.5    Schildkraut, I.6    Saenger, W.7
  • 31
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren, J., Svensson, L.A. and Liljas, A. (1994) Crystal structure of catechol O-methyltransferase. Nature 368, 354-368.
    • (1994) Nature , vol.368 , pp. 354-368
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 32
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier, G., O'Gara, M., Saenger, W. and Cheng, X. (1995) Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247, 16-20.
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4


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