Abstract
Phosphorus deficiency induces the synthesis of acid phosphatases in roots of lupin and other plant species. In this study we examined the induction of secretory acid phosphatase (S-APase) at both the molecular and cellular levels. Lupin plants had increased levels of total acid phosphatase activity within two to five days after P was withered and levels approximately doubled by 15 days. Lateral roots and not main tap roots were responsible for this increase in acid phosphatase activity. Immunoblot analysis using antibodies raised against a purified S-APase showed that the synthesis of this protein was induced as early as 2 days in the P deficient treatment and that levels dramatically increased by 15 days. In contrast, no immunoreactive polypeptide was evident from crude extracts prepared from root tissues of - P treated plants. Immunocytochemical analysis revealed that the protein was located on the surface of epidermal cells of main tap roots and in the cell walls and intercellular spaces of lateral roots and lateral roots may actively secrete S-APase as soon as it is synthesized. A cDNA clone encoding the S-APase was isolated from a cDNA library constructed from lupin roots grown without P. The clone was 2,187 bp in length and had a single open reading frame of 637 amino acid residues. The deduced amino acid sequence was identical to the N-terminal region and peptide sequences of S-APase purified from lupin roots. A hydrophobic signal peptide region consisted of 31 amino acids. The primary structure was highly homologous to iron-zinc purple acid phosphatase from Phaseolus vulgaris (76%), secretory purple acid phosphatase from Arabidopsis thaliana (71%), and two Aspergillus phosphate repressible acid phosphatases (59% and 58%).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Altschul S F, Gish W, Miller W, Myers E W and Lipman D J 1990 Basic local alignment search tool. J. Mol. Biol. 215, 403–410
Bieleski R L and Johnson P N 1972 The external location of phosphatase activity in phosphorus-deficient Spirodela oligorrhiza. Aust. J. Biol. Sci. 25, 707–720
Gish W and States D J 1993 Identification of protein coding regions by database similarity search. Nat. Genet. 3, 266–272
Hein J J 1990 A unified approach to alignment and phylogenies.Methods Enzymol. 183, 626–645
Klabunde T, Stahl B, Suerbaum H, Hahner S, Karas M, Hiillenkamp F, Krebs B and Witzel H 1994 The amino acid sequence of red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Eur. J. Biochem. 226, 369–375
Laemmli U K 1970 Cleavage of structural protein during the assembly of head of bacteriophage T4. Nature 227, 680–685
Li M, Shinano T and Tadano T 1997 Distribution of lupin roots in the rhizosphere under phosphorus deficient conditions. Soil Sci. Plant Nutr. 43, 237–245
Mullaney E J, Daly C B, Ehrlich K C and Ullah A H 1995 The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid phosphatase. Gene 162, 117–121
Ozawa K, Osaki M, Matsui H, Honma M and Tadano T 1995 Purification and properties of acid phosphatase secreted from lupin roots under phosphorus-deficiency conditions. Soil Sci. Plant Nutr. 41, 461–469
Palmiter R D 1974 Magnesium precipitation of ribonucleoprotein complexes. Expedient techniques for the isolation of undegraded polysomes and messenger ribonucleic acid. Biochem. 13, 3606–3615
Saheki S, Takeda A and Shimazu T 1985 Assay of inorganic phosphate in the mild pH range, suitable for measurement ofglycogen phosphorylase activity. Anal. Biochem. 148, 277–281
Sakai H and Tadano T 1993 Characteristics of response of acid phosphatase secreted by the roots of several crops to various conditions in the growth media. Soil Sci. Plant Nutr. 39, 437–444
Sanger F, Nicklen S and Coulson A R 1977 DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463–5467
Tadano T and Sakai H 1991 Secretion of acid phosphatase by the roots of several crop species under phosphorus-deficient conditions. Soil Sci. Plant Nutr. 37, 129–140
Tadano T, Ozawa K, Sakai H, Osaki M and Matsui H 1993 Secretion of acid phosphatase by the roots of crop plants under phosphorus-deficient conditions and some properties of the secreted by lupin roots. Plant and Soil 155/156, 95–98
Tadano T and Komatsu K 1994 Utilization of organic phosphorus in soil by plant roots. Transactions of World Congress of Soil Sci. 9, 521–522
Ueki K and Sato S 1977 Regulation of phosphatse synthesis by orthophsophate in cultured tobacco cells. Plant Cell Physiol. 18, 1253–1263
Ullah A H, Mullaney E M and Dischinger H C Jr. 1994 The complete primary structure elucidation of Aspergillus ficuum (niger), pH 6.0, optimum acid phosphatase by Edman degradation. Biochem. Biophys. Commun. 203, 182–189
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Kluwer Academic Publishers
About this chapter
Cite this chapter
Wasaki, J. et al. (1997). Properties of secretory acid phosphatase from lupin roots under phosphorus-deficient conditions. 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_87
Download citation
DOI: https://doi.org/10.1007/978-94-009-0047-9_87
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6510-8
Online ISBN: 978-94-009-0047-9
eBook Packages: Springer Book Archive