Molecular cloning and characterization of a cDNA that encodes protoporphyrinogen oxidase of Arabidopsis thaliana

Gene

Volumn 182, Issue 1-2, 1996, Pages 169-175

  Narita, Shin Ichiro ^a   Tanaka, Ryouichi ^a   Ito, Toshiro ^a   Okada, Kiyotaka ^a   Taketani, Shigeru ^b   Inokuchi, Hachiro ^a  

^a KYOTO UNIVERSITY   (Japan)

^b KANSAI MEDICAL UNIVERSITY   (Japan)

Author keywords

cDNA library screening; Enzymatic activity; Functional complementation; hemG mutant of Escherichia coli; Leader sequence; Porphyrin biosynthesis

Indexed keywords

COMPLEMENTARY DNA; DNA; MESSENGER RNA; PROTOPORPHYRINOGEN OXIDASE; SIGNAL PEPTIDE; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; BACILLUS SUBTILIS; CONTROLLED STUDY; DNA LIBRARY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE EXPRESSION; GENE ISOLATION; GENETIC COMPLEMENTATION; GENETIC TRANSFORMATION; MOLECULAR CLONING; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PLANT LEAF; PLANT ROOT; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SOUTHERN BLOTTING;

AMINO ACID SEQUENCE; ARABIDOPSIS; BACTERIOPHAGE LAMBDA; BASE SEQUENCE; BLOTTING, NORTHERN; BLOTTING, SOUTHERN; CELL DIVISION; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ESCHERICHIA COLI; GENE EXPRESSION; GENETIC COMPLEMENTATION TEST; GENETIC VECTORS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTATION; NITROBENZOATES; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTOPORPHYRINOGEN OXIDASE; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFORMATION, GENETIC;

ARABIDOPSIS; ARABIDOPSIS THALIANA; BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 17744406796     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(96)00545-8     Document Type: Article

References (21)

1. Bach, A.W.J., Lan, N.C., Johnson, D.L., Abell, C.W., Bembenek, M.E., Kwan, S.W., Seeburg, P.H. and Shih, J.C. (1988) cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc. Natl. Acad. Sci. USA 85, 4934-4938.
2. 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.
3. Brandsch, R., Hinkkanen, A.E., Mauch, L., Nagursky, H. and Decker, K. (1987) 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur. J. Biochem. 167, 315-320.
4. Camadro, J.-M., Matringe, M., Scalla, R. and Labbe, P. (1991) Kinetic studies on protoporphyrinogen oxidase inhibition by diphenyl ether herbicides. Biochem. J. 277, 17-21.
5. Dailey, H.A. (1990) Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: terminal three enzymes. In: Dailey, H.A. (Ed.), Biosynthesis of Heme and Chlorophylls. McGraw-Hill, New York, pp. 123-162.
6. Fleischmann, R.D., Adams, M.D., White, O., Clayton, R.A., Kirkness, E.F., Kerlavage, A.R., Bult, C.J., Tomb, J.-F., Dougherty, B.A., Merrick, J.M. et al. (1995) Whole genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269, 496-512.
7. Gari, E., Toledo, J.C., Gibert, I. and Barbe, J. (1992) Nucleotide sequence of the methoxyneurosporene dehydrogenase gene from Rhodobacter sphaeroides: comparison with other bacterial carotenoid dehydrogenases. FEMS Microbiol. Lett. 72, 103-108.
8. Hansson, M. and Hederstedt, L. (1992) Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 174, 8081-8093.
9. Ito, A., Kuwahara, T., Inadome, S. and Sagara, Y. (1988) Molecular cloning of a cDNA for rat liver monoamine oxidase B. Biochem. Biophys. Res. Commun. 157, 970-976.
10. Jacobs, J.M., Jacobs, N.J. and De Maggio, A.E. (1982) Protoporphyrinogen oxidation in chloroplasts and plant mitochondria, a step in heme and chlorophyll synthesis. Arch. Biochem. Biophys. 218, 233-239.
11. Klemm, D.J. and Barton, L.L. (1987) Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas. J. Bacteriol. 169, 5209-5215.
12. Lang, H., Polster, M. and Brandsch, R. (1991) Rat liver dimethylglycine dehydrogenase. Flavinylation of the enzyme in hepatocytes in primary culture and characterization of a cDNA clone. Eur. J. Biochem. 198, 793-799.
13. Matringe, M., Camadro, J.-M., Labbe, P. and Scalla, R. (1989) Protoporphyrinogen oxidase as a molecular target for diphenyl ether herbicides. Biochem. J. 260, 231-235.
14. Nishimura, K., Nakayashiki, T. and Inokuchi, H. (1995a) Cloning and identification of the hemG gene encoding protoporphyrinogen oxidase (PPO) of Escherichia coli K-12. DNA Res. 2, 1-8.
15. Nishimura, K., Taketani, S. and Inokuchi, H. (1995b) Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli. J. Biol. Chem. 270, 8076-8080.
16. Nordmann, Y. and Deybach, J.-C. (1990) Human hereditary porphyrias. In: Dailey, H.A. (Ed.), Biosynthesis of Heme and Chlorophylls. McGraw-Hill, New York, pp. 491-542.
17. 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.
18. Taketani, S., Yoshinaga, T., Furukawa, T., Kohno, H., Tokunaga, R., Nishimura, K. and Inokuchi, H. (1995) Induction of terminal enzymes for heme biosynthesis during differentation of mouse erythroleukemia cells. Eur. J. Biochem. 230, 760-765.
19. Van Beeumen, J.J., Demol, H., Samyn, B., Bartsch, R.G., Meyer, T.E., Dolata, M.M. and Cusanovich, M.A. (1991) Covalent structure of the diheme cytochrome subunit and amino-terminal sequence of the flavoprotein subunit of flavocytochrome c from Chromatium vinosum. J. Biol. Chem. 266, 12921-12931.
20. Von Heijne, G. (1986) Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5, 1335-1342.
21. Witkowski, D.A. and Halling, B.P. (1989) Inhibition of plant protoporphyrinogen oxidase by the herbicide acifluorfen-methyl. Plant Physiol. 90, 1239-1242.