Either soluble or plastidic expression of recombinant protoporphyrinogen oxidase modulates tetrapyrrole biosynthesis and photosynthetic efficiency in transgenic rice

Bioscience, Biotechnology and Biochemistry

Volumn 67, Issue 7, 2003, Pages 1472-1478

  Jung, Sunyo ^a   Chung, Jung Sung ^b   Jang, Sun Mi ^b   Guh, Ja Ock ^b   Lee, Hee Jae ^c   Chon, Sang Uk ^d   Kim, Kyung Moon ^a   Ha, Suk Bong ^b   Back, Kyoungwhan ^b  

^a Scigen Harvest Research Center   (South Korea)

^b Chonnam National University   (South Korea)

^c Seoul National University   (South Korea)

^d Dongshin University   (South Korea)

Author keywords

Bacillus subtilis; Photosynthetic activity; Protoporphyrin IX; Protoporphyrinogen oxidase; Transgenic rice

Indexed keywords

BACILLUS SUBTILIS;

AMINOLEVULINIC ACID; CARBON DIOXIDE; CHLOROPHYLL; HEME; MESSENGER RNA; OXIDOREDUCTASE; PROTOPORPHYRINOGEN OXIDASE; RECOMBINANT PROTEIN; TETRAPYRROLE DERIVATIVE;

ARTICLE; BACILLUS SUBTILIS; BIOSYNTHESIS; ENZYMOLOGY; GENE EXPRESSION; GENE VECTOR; GENETICS; METABOLISM; PHOTOSYNTHESIS; PHYSIOLOGY; PLASTID; RICE; SOLUBILITY; TRANSGENIC PLANT; WESTERN BLOTTING;

AMINOLEVULINIC ACID; BACILLUS SUBTILIS; BLOTTING, WESTERN; CARBON DIOXIDE; CHLOROPHYLL; GENE EXPRESSION; GENETIC VECTORS; HEME; ORYZA SATIVA; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PHOTOSYNTHESIS; PLANTS, GENETICALLY MODIFIED; PLASTIDS; PROTOPORPHYRINOGEN OXIDASE; RECOMBINANT PROTEINS; RNA, MESSENGER; SOLUBILITY; TETRAPYRROLES;

EID: 2442430367     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.1472     Document Type: Article

References (29)

1. Beale, S. I., and Weinstein, J. D., Tetrapyrrole metabolism in photosynthetic organisms. In “Biosynthesis of Heme and Chlorophylls”, ed. Dailey, H. A., McGraw Hill, New York, pp. 287-391 (1990).
2. Jacobs, J. M., Jacobs, N. J., Borotz, S. E., and Guerinot, M. L., Effects of the photobleaching herbicide, acifluorfen-methyl, on protoporphyrinogen oxidation in barley organelles, soybean root mitochondria, soybean root nodules, and bacteria. Arch. Biochem. Biophys., 280, 369-375 (1990).
3. Jacobs, J. M., and Jacobs, N. J., Porphyrinogen accumulation and export by isolated barley (Horde-um vulgare L.) plastids. Plant Physiol., 101, 1181-1187 (1993).
4. Smith, A. G., Marsh, O., and Helder, G. H., Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochem. J., 292, 503-508 (1993).
5. Lee, H. J., Ball, M. D., and Rebeiz, C. A., In-traplastidic localization of the enzymes that convert d-aminolevulinic acid to protoporphyrin IX in etiolated cucumber cotyledons. Plant Physiol., 96, 910-915 (1991).
6. Matringe, M., Camadro, J. M., Block, M. A., Joyard, J., Scalla, R., Labbe, P., and Douce, R., Localization within chloroplasts of protoporphyrinogen oxidase, the target enzyme for diphenyl ether-like herbicides. J. Biol. Chem., 267, 4646-4651 (1992).
7. Choi, K. W., Han, O., Lee, H. J., Yun, Y. C., Moon, Y. H., Kim, M., Kuk, Y. I., Han, S. U., and Guh, J. O., Generation of resistance to the diphenyl ether herbicide, oxyfluorfen, via expression of the Bacillus subtilis protoporphyrinogen oxidase gene in transgenic tobacco plants. Biosci. Biotechnol. Biochem., 62, 558-560 (1998).
8. Lermontova, I., and Grimm, B., Overexpression of plastidic protoporphyrinogen IX oxidase leads to resistance to the diphenyl-ether herbicide acifluorfen. Plant Physiol., 122, 75-83 (2000).
9. Lee, H. J., Lee, S. B., Chung, J. S., Han, S. U., Han, O., Guh, J. O., Jeon, J. S., An, G., and Back, K., Transgenic rice plants expressing a Bacillus subti-lis protoporphyrinogen oxidase gene are resistant to diphenyl ether herbicide oxyfluorfen. Plant Cell Physiol., 41, 743-749 (2000).
10. Duke, S. O., Nandihalli, U. B., Lee, H. J., and Duke, M. V., Protoporphyrinogen oxidase as the optimal herbicide site in the porphyrin pathway. Amer. Chem. Soc. Symp. Ser., 559, 191-204 (1994).
11. Matsumoto, H., Tanida, Y., and Ishizuka, K., Porphyrin intermediate involved in herbicidal action of d-aminolevulinic acid on duckweed (Lemna pausicostata Helgelm.). Pestic. Biochem. Physiol., 48, 214-221 (1994).
12. Lee, H. J., Duke, M. V., and Duke, S. O., Cellular localization of protoporphyrinogen-oxidizing activities of etiolated barley (Hordeum vulgare L.) leaves: relationship to mechanism of action of protoporphyrinogen oxidase-inhibiting herbicides. Plant Physiol., 102, 881-889 (1993).
13. Scalla, R., and Matringe, M., Inhibitors of protoporphyrinogen oxidase as herbicides: diphenyl ethers and related photobleaching molecules. Rev. Weed Sci., 6, 103-132 (1994).
14. Back, K., Yin, S., and Chappell, J., Expression of a plant sesquiterpene cyclase gene in Escherichia coli. Arch. Biochem. Biophys., 315, 527-532 (1994).
15. Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: a laboratory mannul, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1989).
16. Guo, R., Lim, C. K., and Peters, T. J., High-performance liquid chromatographic assays for protoporphyrinogen oxidase and ferrochelatase in human leucocytes. J. Chromatogr., 566, 383-396 (1991).
17. Lichtenthaler, H. K., Chlorophylls and carotenoids: pigments of photosynthetic biomembranes. Methods Enzymol., 148, 350-382 (1987).
18. Papenbrock, J., Mock, H. P., Kruse, E., and Grimm, B., Expression studies in tetrapyrrole biosynthesis: inverse maxima of magnesium chelatase and ferrochelatase activity during cyclic photoperiods. Planta, 208, 264-273 (1999).
19. Kruse, E., Mock, H. P., and Grimm, B., Reduction of coproporphyrinogen III oxidase level by antisense RNA synthesis leads to deregulated gene expression of plastid proteins and affects the oxidative defense system. EMBO J., 14, 3712-3720 (1995).
20. Schneegurt, M. A., and Beale, S. I., Biosynthesis of protoheme and heme a from glutamate in maize. Plant Physiol., 81, 965-971 (1986).
21. Genty, B., Briantais, J. M., and Baker, N., The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence. Biochem. Biophys. Acta, 990, 87-92 (1989).
22. Beale, S. I., d-Aminolevulinic acid in plants: Its biosynthesis, regulation, and role in plastid development. Annu. Rev. Plant Physiol., 29, 95-120 (1978).
23. Cure, J. D., and Acock, B., Crop responses to carbon dioxide doubling: a literature survey. Agric. For Meteorol., 38, 127-145 (1986).
24. 2 concentration. Vegetatio., 104/105, 77-97 (1993).
25. 2. Plant Physiol., 115, 15-22 (1997).
26. Hotta, Y., Tanaka, T., Takaoka, H., Takeuchi, Y., and Konnai, M., Promotive effects of 5-aminolevulin-ic acid on the yield of several crops. Plant Growth Regul., 22, 109-114 (1997).
27. Thiele, A., Herold, M., Lenk, I., Quail, P. H., and Gatz, C., Heterologous expression of Arabidopsis phytochrome B in transgenic potato influences photosynthetic performance and tuber development. Plant Physiol., 120, 73-81 (1999).
28. Suzuki, S., Murai, N., Burnell, J. N., and Arai, M., Changes in photosynthetic carbon in transgenic rice plants that express C4-type phosphoenolpyruvate carboxykinase from Urochloa panicoides. Plant Physiol., 124, 163-172 (2000).
29. 4 (Pani-cum antidotale) grass. Aust. J. Plant Physiol., 24, 227-237 (1997).