Abstract
This paper reviewes recent work on the cloning genes encoding enzymes in the biosynthetic pathway of the mugineic acid family of phytosiderophores or the trial of the cloning of Fe (III)-MAs transporter. The Fe-deficiency induced genes which have been cloned in barley roots are nicotianamine aminotransferase (naat), formate dehydrogenase (Fdh), adenine phosphoribosyl-transferase (Aprt), alcoholdehydrogenase (Adh), and the iron deficiency specific clones Ids1, Ids2 and Ids3. SAM synthetase (sam) was not induced by Fe deficiency. Genes of nicotianamine synthetase (nas) and a 36kD-peptide were not successfully cloned. The physiological importance of these genes are discussed.
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References
Butt T R, Steinberg E J, Gorman J A, Clark P, Hamer D, Rosenberg M and Crooke S T 1984 Copper metallothionein of yeast, structure of the gene, and regulation of expression. Proc. Natl. Acad. Sci. (USA) 81, 3332–3336.
Dancis A, Yuan D S, Haile D, Askwith C, Eide D, Moehle, Kaplan J and Klausner R D 1994 Molecular chracterization of a copper transport protein in Saccharomyces cerevisiae: Un unexpected role for copper in iron transport. Cell 76, 393–402.
Ferry J G 1990 Formate dehydrogenase. FEMS Microbiol Rev. 87, 377–382
George A 1996 Regulation of release of phytosiderophores in barley and wheat under iron and zinc deficiency. PhD theses, Verlag Ulrich E. Grauer’Stuttgart’
Herbik A, Giritch A, Horstmann C, Becker R, Balzer H-J, Baumlein H and Stephan U W 1996 Iron and copper nutrition-dependent changes in protein expression in a tomato wild type and the nicotianamine-free mutant chloronerva. Plant Physiol. 111, 533–540.
Higuchi K, Kanazawa K, Nishizawa N K, Chino M and Mori S 1994 Purification and characterization of nicotianamine synthase from Fe deficient barley roots. Plant and Soil 165, 173–179.
Higuchi K, Kanazwa K, Nishizawa N K and Mori S 1996 The role of nicotianamine synthase in response to Fe nutrition status in Gramineae. Plant and Soil 178, 171–177.
Huang C, Graham R D, Barker S J and Mori S 1996 Differential expression of iron deficiency-induced genes in barley genotypes with different manganese deficiency. J. Plant Nutr. 19, 407–420
Kanazawa K, Higuchi K, Fushiya S, Nishizawa N K, Chino M and Mori S 1994 Induction of two enzyme activities involved in the biosynthesis of mugineic acid in Fe deficient barley roots. In Iron Nutrition in Soils and Plants. Ed. J Abadia. pp 37–41. Netherland.
Kanazawa K, Higuchi K, Nishizawa N-K, Fushiya S and Mori S 1995 Detection of two distinct isozymes of nicotianamine aminotransferases in Fe-deficient barley roots. J. Exp. Botany 46, 1241–1244
Lam E, Benfay P N, Gilmartin P M, Fang R-X and Chua N-H 1989 Site specific mutations alter in vitro factor binding and change promoter expression pattern in transgenic plants. Proc. Natl. Acad. Sci. 86, 7890–7894.
Ma J F and Nomoto K 1993 Two related biosynthetic pathways of mugineic acids in gramineous plants. Plant Physiol. 102, 373–378.
Ma J F, Shinada T, Matsuda C and Nomoto K 1995 Biosysnthesis of phytosiderophores, mugineic acids, associated with methionine cycling. J. Biol. Chem. 270, 16549–16554
Masui H 1991 Increase in activity of NADH oxidase system and development of mitochondrial structure by recovering from iron-deficiency in Saccharomyces cerevisiae. J. Sci. Hiroshima Univ., Ser. B, Div 2, 23, 369–376.
Mitchell L E, Dennis E S and Peacock W J 1989 Molecular analysis of an alcohol dehydrogenasae (Adh) gene from chromosome 1 of wheat. Genome 32, 349–358.
Mori S, Nishizawa N K and Fujigaki J 1990 Identification of rye chromosome-5R as a carrier of the genes for mugineic acid synthetase and 3-hydroxymugineic acid sythetase using wheat-rye addition lines. Jpn. J. Genet. 65, 343–352.
Mori S and Nishizawa N 1987 Methionine as a dominant precursor of phytosiderophores in Gramineae plants. Plant Cell Physiol 28, 1081–1092.
Mori S and Nishizawa N 1989 Identification of barley chromosome no.4, possible encoder of genes of mugineic acid synthetase from 2’-deoxymugineic acid using wheat-barley addition line. Plant Cell Physiol. 30, 1057–1061.
Mori S, Nishizawa N, Hayashi H, Chino M, Yoshimura E, and Ishihara J 1991 Why are young rice plants highly susceptible to iron deficiency? Plant and Soil 130, 143–156.
Mori S 1994 Mechanism of Iron Acquisition by Gramineous (Strategy II) Plants. In Biochemistry of Metal Micronutrients in the Rhizosphere. pp 225–249. Eds. J A Manthey, D E Crowley and D G Luster. Lewis Publishers.
Nakanishi H, Okumura N, Umehara Y, Nishizawa N K, Chino M and Mori S 1993 Expression of a gene specific for iron deficiency (Ids3) in the roots of Hordeum vulgare. Plant Cell Physiol 34, 401–410.
Ohata T, Kanazawa K, Mihashi S, Nishizawa N K, Fushiya S, Nozoe S, Chino M and Mori S 1993 Biosynthetic pathway of phytosiderophores in iron-deficient graminaceous plants; Establishment of an assay system for the detection of nicotianamine aminotransferase activity. Soil Sci. Plant Nutr. 39, 745–749.
Okumura N, Nishizawa N K, Umehra Y and Mori S 1991 An iron deficiency-specific cDNA from barley roots having two homologous cystein-rich MT domains. Plant Mol. Biol. 17, 531–533.
Okumura N, Nishizawa N K, Umehara Y, Ohata T, Nakanishi H, Yamaguchi T, Chino M and Mori S 1994 A dioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare. Plant Mol. Biol. 25, 705–719.
Peleman J, Boerjan W, Engler G, Seurinck J, Botterman J, Alliotte T, Montague M V and Nnze D 1989 Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase. Plant Cell 1, 81–93.
Prescot A G 1996 Dioxygenases: Molecular structure and role in plant metabolism. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 245–271
Römheld V and Marschner H 1986 Evidence for a specific uptake system for iron phytosiderophore in roots of grasses. Plant Physiol. 80, 175–180.
Shojima S, Nishizawa N K, Fushiya S, Nozoe S, Kumashiro T, Nagata T, Ohata T and Mori S 1989 Biosynthesis of nicotianamine in the suspension-cultured cells of tobacco (Nicotiana megalosiphon). Biol. Metals 2, 142–145.
Shojima S, Nishizawa N K, Fushiya S, Irifune T and Mori S 1990 Biosynthesis of phytosiderophores. In vitro biosynthesis of 2’-deoxymugineic acid from L-methionine and nicotianamine. Plant Physiol. 93, 1497–1503.
Suzuki K, Hirano H, Yamaguchi H, Irifune T, Nishizawa N K, Chino M and Mori S 1995 Partial amino acid sequences of a peptide induced by Fe deficiency in barley roots. In Iron Nutrition in Soils and Plants. Ed. J Abadia. pp 363–369. Kluwer Academic Publishers, Netherlands.
Suzuki K, Kanazawa K, Higuchi K, Nishizawa N-K and Mori S 1997 Immunological characterization of a 36 kDa Fe-deficiency specific peptide in barley roots. Bio Metals 10, 77–84.
Takagi S 1976 Naturally occurring iron-chelating compounds in oat-and rice-root washing. I. Soil Sci. Plant Nutr. 22, 423–433.
Takagi S, Nomoto K and Takemoto T 1984 Physiological aspect of mugineic acid, a possible phytosiderophore of graminaceous plants. J. Plant Nutr. 7, 469–477.
Takagi S 1993 Production of phytosiderophores. In Iron Chelation in Plants and Soil Microorganisms. Eds. L Barton and H Hemming. pp 111–131. Academic Press, New York
Takizawa R, Nishizawa N-K, Nakanishi H and Mori S 1996 Effect of iron deficiency on S-adenosylmethionine synthetase in barley roots. J. Plant Nutr. 19, 1189–1200
Trick M, Dennis E S, Edward K J R and Peacock W J 1988 Molecular analysis of the alcohol dehydrogenase gene family of barley. Plant Mol. Biol. 11, 147–160.
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Mori, S. (1997). Reevaluation of the genes induced by iron deficiency in barley roots. In: Ando, T., Fujita, K., Mae, T., Matsumoto, H., Mori, S., Sekiya, J. (eds) Plant Nutrition for Sustainable Food Production and Environment. Developments in Plant and Soil Sciences, vol 78. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0047-9_67
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DOI: https://doi.org/10.1007/978-94-009-0047-9_67
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