|
|
|
|
|
| Molecular Characterization and Functional Analysis of OsPHY1, a Purple Acid Phosphatase (PAP)-Type Phytase Gene in Rice (Oryza sativa L.) |
| LI Rui-juan, LU Wen-jing, GUO Cheng-jin, LI Xiao-juan, GU Jun-tao, XIAO Kai |
1.College of Life Sciences, Agricultural University of Hebei, Baoding 071001, P.R.China
2.College of Agronomy, Agricultural University of Hebei, Baoding 071001, P.R.China |
|
|
|
摘要 As a specific type of acid phosphatses, phytases play diverse roles in plants by catalazing the degradation of phytic acid and its derivatives. In this study, a rice phytase gene referred to OsPHY1 has been functionally characterized. OsPHY1 contains a 1 620 bp of open reading frame, encoding a 539-aa polypeptide. A conserve domain metallophosphatase (MPP) (MPP_PAPs), generally harbored in phytase and purple acid phosphatases (PAP), was identified in OsPHY1 (residue 194- 398). Phylogenetic analysis revealed that OsPHY1 shares high similarities with phytase genes and PAP-type genes that derived from diverse plant species. The OsPHY1 transcripts were detected to be abundant in germinating seeds, suggesting that this gene plays potential roles on degradation of seed phytic acid and its derivatives during the germination process. Biochemical analysis confirmed that OsPHY1 possesses strong catalytic activities on phytic acid-Na2, with optimal temperature of 57°C and suitable pH of 3.5. Based on transgene analysis, the putative role of OsPHY1 in plants on utilization of phytate was assessed. Under the condition that phytic acid-Na2 was used as sole P source, the OsPHY1- overexpressing tobacco plants behaved higher phytase activities, higher concentrations of Pi, more accumulative amount of total phosphorus, and much more improved growth traits than those of the control plants. Therefore, OsPHY1 is acted as an important component on degradation of the phytins during the seed germination process in rice. Also, OsPHY1 has a potential use on generation of elite crop germplasms with improved use efficiencies on phytate and its derivatives.
Abstract As a specific type of acid phosphatses, phytases play diverse roles in plants by catalazing the degradation of phytic acid and its derivatives. In this study, a rice phytase gene referred to OsPHY1 has been functionally characterized. OsPHY1 contains a 1 620 bp of open reading frame, encoding a 539-aa polypeptide. A conserve domain metallophosphatase (MPP) (MPP_PAPs), generally harbored in phytase and purple acid phosphatases (PAP), was identified in OsPHY1 (residue 194- 398). Phylogenetic analysis revealed that OsPHY1 shares high similarities with phytase genes and PAP-type genes that derived from diverse plant species. The OsPHY1 transcripts were detected to be abundant in germinating seeds, suggesting that this gene plays potential roles on degradation of seed phytic acid and its derivatives during the germination process. Biochemical analysis confirmed that OsPHY1 possesses strong catalytic activities on phytic acid-Na2, with optimal temperature of 57°C and suitable pH of 3.5. Based on transgene analysis, the putative role of OsPHY1 in plants on utilization of phytate was assessed. Under the condition that phytic acid-Na2 was used as sole P source, the OsPHY1- overexpressing tobacco plants behaved higher phytase activities, higher concentrations of Pi, more accumulative amount of total phosphorus, and much more improved growth traits than those of the control plants. Therefore, OsPHY1 is acted as an important component on degradation of the phytins during the seed germination process in rice. Also, OsPHY1 has a potential use on generation of elite crop germplasms with improved use efficiencies on phytate and its derivatives.
|
|
Received: 01 April 2011
Accepted:
|
| Fund: This work was supported by the National Natural Science Foundation of China (30871466) and the Key Laboratory of Crop Growth Regulation of Hebei Province, China. |
|
Corresponding Authors:
Correspondence XIAO Kai, Tel: +86-312-7528115, Fax: +86-312-7528400, E-mail: xiaokai3@yahoo.com
E-mail: xiaokai3@yahoo.com
|
Cite this article:
LI Rui-juan, LU Wen-jing, GUO Cheng-jin, LI Xiao-juan, GU Jun-tao, XIAO Kai.
2012.
Molecular Characterization and Functional Analysis of OsPHY1, a Purple Acid Phosphatase (PAP)-Type Phytase Gene in Rice (Oryza sativa L.). Journal of Integrative Agriculture, 12(8): 1217-1226.
|
| [1]Ames B N. 1966. Assay of inorganic phosphate, total phosphate and phosphatases. In: Neufeld E, Ginsburg V, eds., Methods in Enzymology. Academic Press, New York, USA. pp. 115-118. [2]Asmar F. 1997. Variation in activity of root extracellular phytase between genotypes of barley. Plant Soil, 195, 61-64. [3]Dionisio G, Holm P B, Brinch-Pedersen H. 2007. Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination. Plant Biotechnology Journal, 5, 325-338. [4]Flanagan J U, Cassady A I, Schenk G, Guddat L W, Hume D A. 2006. Identification and molecular modeling of a novel, plant-like, human purple acid phosphatase. Gene, 377, 12-20. [5]Goldstein A H, Baertlein D A, McDaniel R G. 1988. Phosphate starvation inducible metabolism in Lycopersicon esculentum. 1. Excretion of acidphosphatase by tomato plants and suspension-cultured cells. Plant Physiology, 87, 711-715. [6]Guo L, Zhao Y X, Zhang S H, Zhang H N, Xiao K. 2009. Improvement of organic phosphate acquisition in transgenic tobacco plants by overexpression of a soybean phytase gene Sphy1. Frontiers of Agriculture in China, 3, 259-265. [7]Hayes J E, Richardson A E, Simpson R J. 1999. Phytase and acid phosphatase activities in extracts from roots of temperate pasture grass and legume seedlings. Australian Journal of Plant Physiology, 26, 801-809. [8]Hegeman C E, Grabau E A. 2001. A novel phytase with sequence similarity to purple acid phosphatases is expressed in cotyledons of germinating soybean seedlings. Plant Physiology, 126, 1598-1608. [9]Lambers H, Shane M W, Cramer M D, Pearse S J, Veneklaas E J. 2006. Root structure and functioning for efficient acquisition of phosphorus: matching morphological and physiological traits. Annals of Botany, 98, 693-713. [10]Li D, Zhu H, Liu K, Liu X, Leggewie G, Udvardi M, Wang D. 2002. Purple acid phosphatases of Arabidopsis thaliana: comparative analysis and differential regulation by phosphate deprivation. Journal of Biological Chemistry, 277, 27772-27781. [11]Li M, Osaki M, Rao I M, Tadano T. 1997. Secretion of phytase from the roots of several plant species under phosphorus-deficient conditions. Plant Soil, 195, 161-169. [12]Loewus F A, Murthy P P N. 2000. Myo-inositol metabolism in plants. Plant Science, 150, 1-19. [13]Lott J N A, Greenwood J S, Batten B D. 1995. Mechanisms and regulation of mineral nutrient storage during seed development. In: Kigel J, Galili G, eds., Seed Development and Germination. Marcel Dekker, New York, USA. pp. 215-235. [14]Lung S C, Leung A, Kuang R, Wang Y, Leung P, Lim B L. 2008. Phytase activity in tobacco (Nicotiana tabacum) root exudates is exhibited by a purple acid phosphatase. Phytochemistry, 69, 365-373. [15]Maugenest S, Martinez I, Lescure A M. 1997. Cloning and characterization of a cDNA encoding a maize seedling phytase. Biochemical Journal, 322, 511-517. [16]Mehta B D, Jog S P, Johnson S C, Murthy P P. 2006. Lily pollen alkaline phytase is a histidine phosphatase similar to mammalian multiple inositol polyphosphate phosphatase (MINPP). Phytochemistry, 67, 1874-1886. [17]Mimura T. 1999. Regulation of phosphate transport and homeostasis in plant cells. International Review of Cytology, 191, 149-200. [18]Morgan M A. 1997. The Behaviour of Soil and Fertilizer Phosphorus. CAB International, Oxon, UK. Mudge S R, Rae A L, Diatloff E, Smith F W. 2002. Expression analysis suggests novel roles for members of the Pht1 family of phosphate transporters in Arabidopsis. Plant Journal, 31, 341-353. [19]Mullaney E J, Ullah A H. 2003. The term phytase comprises several different classes of enzymes. Biochemical and Biophysical Research Communications, 312, 179-184. [20]Murashige T, Skoog F. 1962. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiologia Plantarum, 15, 473-497. [21]Oelkers E H, Valsami-Jones E. 2008. Phosphate mineral reactivity and global sustainability. Elements, 4, 83-87. [22]Raboy V. 1997. Accumulation and storage of phosphate and minerals. In: Larkins B A, Vasil I K, eds., Cellular and Molecular Biology of Plant Seed Development. Kluwer Academic Publishers, Dordrecht, The Netherlands. pp. 441-477. [23]Raghothama K G. 1999. Phosphate acquisition. Annual Review of Plant Physiology and Plant Molecular Biology, 50, 665-693. [24]Richardson A E, Hadobas P A, Hayes J E. 2001. Extracellular secretion of Aspergillus phytase from Arabidopsis roots enables plants to obtain phosphorus from phytate. Plant Journal, 25, 641-649. [25]Schachtman D P, Reid R J, Ayling S M. 1998. Phosphorus uptake by plants: from soil to cell. Plant Physiology, 116, 447-453. [26]Sharpley A N, Chapra S C, Wedepohl R, Sims J T, Daniel T C, Reddy K R. 1994. Managing agricultural phosphorus for protection of surface waters-issues and options. Journal of Environmental Quality, 23, 437-451. [27]Shenoy V V, Kalagudi G M. 2005. Enhancing plant phosphorus use efficiency for sustainable cropping. Biotechnology Advances, 23, 501-513. [28]Vance C P, Uhde-stone C, Allan D L. 2003. Phosphorus acquisition and use: critical adaptations by plants for securing a nonrenewable resource. New Phytologist, 157, 423-447. [29]Vincent J B, Crowder M W, Averill B A. 1992. Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends in Biochemical Sciences, 17, 105-110. [30]Wodzinski R J, Ullah A H J. 1996. Phytases. Advances in Applied Microbiology, 42, 263-302. [31]Xiao K, Harrison M J, Wang Z Y. 2005. Transgenic expression of a novel M. truncatula phytase gene results in improved acquisition of organic phosphorus by Arabidopsis. Planta, 222, 27-36. [32]Xiao K, Katagi H, Harrison M, Wang Z Y. 2006. Improved phosphorus acquisition and biomass production in Arabidopsis by transgenic expression of a purple acid phosphatase gene from M. truncatula. Plant Science, 170, 191-202. [33]Zhang W Y, Gruszewski H A, Chevone B I, Nessler C L. 2007. An Arabidopsis purple acid phosphatase with phytase activity increases foliar ascorbate. Plant Physiology, 146, 431-440. |
| No Suggested Reading articles found! |
|
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
| |
Shared |
|
|
|
|
| |
Discussed |
|
|
|
|
