GmPAP3, a novel purple acid phosphatase-like gene in soybean induced by NaCl stress but not phosphorus deficiency

Gene

Volumn 318, Issue 1-2, 2003, Pages 103-111

  Liao, Hong ^a,b   Wong, Fuk Ling ^a   Phang, Tsui Hung ^a   Cheung, Ming Yan ^a   Li, Wing Yen Francisca ^a   Shao, Guihua ^a,c   Yan, Xiaolong ^b   Lam, Hon Ming ^a  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

^b SOUTH CHINA AGRICULTURAL UNIVERSITY   (China)

^c INSTITUTE OF PLANT PROTECTION   (China)

Author keywords

Gene expression; Glycine max; Glycine soja; PAP

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; REACTIVE OXYGEN METABOLITE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; GENE EXPRESSION; GENE IDENTIFICATION; MITOCHONDRION; MOLECULAR PHYLOGENY; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; OXIDATIVE STRESS; PHOSPHATE DEFICIENCY; PLANT GENETICS; PLANT LEAF; PLANT ROOT; PRIORITY JOURNAL; PROTEIN TARGETING; SALT STRESS; SIGNAL TRANSDUCTION; SOYBEAN; TECHNIQUE;

ANIMALIA; FUNGI; GLYCINE MAX; GLYCINE SOJA;

EID: 0242285640     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00764-9     Document Type: Article

References (44)

1. Bannai H., Tamada Y., Maruyama O., Nakai K., Miyano S. Extensive feature detection of N-terminal protein sorting signals. Bioinformatics. 18:2002;298-305.
2. Beck J.L., McConachie L.A., Summors A.C., Arnold W.N., Dejersey J., Zerner B. Properties of a purple acid phospatase from red kidney bean: a zinc-iron metalloenzyme. Biochim. Biophys. Acta. 869:1986;61-68.
3. Bohnert H.J., Su H., Shen B. Molecular mechanisms of salinity tolerance. Kazuo S., Kazuko Y.S. Molecular Responses to Cold, Drought, Heat and Salt Stress in Higher Plants. 1999;29-60 R.G. Landes, Austin.
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
5. Cashikar A.G., Kumaresan R., Rao N.M. Biochemical characterization and subcellular localization of the red kidney bean purple acid phosphatase. Plant Physiol. 114:1997;907-915.
6. Casolo V., Braidot E., Chiandussi E., Macri F., Vianello A. The role of mild uncoupling and non-coupled respiration in the regulation of hydrogen peroxide generation by plant mitochondria. FEBS Lett. 474:2000;53-57.
7. Dat J., Vandenabeele S., Vranova E., Van Montagu M., Inze D., Van Breusegem F. Dual action of the active oxygen species during plant stress responses. Cell. Mol. Life Sci. 57:2000;779-795.
8. del Pozo J.C., Allona I., Rubio V., Leyva A., Pena A.D.L., Aragoncillo C., Paz-Ares J. A type 5 acid phosphatase gene from Arabidopsis thaliana is induced by phosphate starvation and by some other types of phosphate mobilising/oxidative stress conditions. Plant J. 19:1999;579-589.
9. +) or total RNA. Siebert P., Larrick J. RT-PCR Method for Gene Cloning and Analysis. 1998;213-239 Eaton Publishing, Natick, MA.
10. Duff S.M.G., Sarath G., Plaxton W.C. The role of acid phosphatases in plant phosphorus metabolism. Physiol. Plant. 90:1994;791-800.
11. Durmus A., Eicken C., Spener F., Krebs B. Cloning and comparative protein modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas). Biochim. Biophys. Acta. 1434:1999;202-209.
12. Emanuelsson O., Nielsen H., Brunak S., von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300:2000;1005-1016.
13. Finckh U., Lingenfelter P.A., Myerson D. Producing single-stranded DNA probes with the Taq DNA polymerase: a high yield protocol. Biotechniques. 10:1991;35-38.
14. Gueta-Dahan Y., Yaniv Z., Zilinskas B.A., Ben-Hayyim G. Salt and oxidative stress: similar and specific responses and their relation to salt tolerance in Citrus. Planta. 203:1997;460-469.
15. Hegeman C.E., Grabau E.A. A novel phytase with sequence similarity to purple acid phosphatases is expressed in cotyledons of germinating soybean seedlings. Plant Physiol. 126:2001;1598-1608.
16. Hoagland D.R., Arnon D.I. The water-culture method for growing plants without soil. Calif. Agric. Expt. Circ. 347:1938;1-39.
17. Igaue I., Watabe H., Takahashi K., Takahashi M., Morota A. Violet-colored acid phosphatase isozymes associated with cell wall preparariom rice plant cultured cells. Agric. Biol. Chem. 40:1976;823-825.
18. Jackson A.O., Larkins B.A. Influence of ionic strength, pH, and chelation of divalent metals on isolation of polyribosomes from tobacco leaves. Plant Physiol. 57:1976;5-10.
19. Jiang M., Zhang J. Water stress-induced abscisic acid accumulation triggers the increased generation of reactive oxygen species and up-regulates the activities of antioxidant enzymes in maize leaves. J. Exp. Bot. 53:2002;2401-2410.
20. Kennedy B.F., De Filippis L.F. Physiological and oxidative response to NaCl of the salt tolerant Grevillea ilicifolia and the salt sensitive Grevillea arenaria. J. Plant Physiol. 155:1999;746-754.
21. Klabunde T., Stahl B., Suerbaum H., Hahner S., Karas M., Hillenkamp F., Krebs B., Witzel H. The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase. Determination of the amino acid sequence by a combination of matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing. Eur. J. Biochem. 226:1994;369-375.
22. Klabunde T., Strater N., Krebs B., Witzel H. Structural relationship between the mammalian Fe(III)-Fe(II) and Fe(III)-Zn(II) plant purple acid phosphatases. FEBS Lett. 367:1995;56-60.
23. Klabunde T., Strater N., Witzel H., Frohlich R., Krebs B. Mechanism of Fe(III)-Zn(II) purple acid phosphatases based on crystal structures. J. Mol. Biol. 259:1996;737-748.
24. Kumar S., Tamura K., Jakobsen I.B., Nei M. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics. 17:2001;1244-1245.
25. LeBansky B.R., Mcknight T., Griffing L.R. Purification and characterization of a secreted purple phosphatase from soybean suspension culture. Plant Physiol. 99:1992;391-395.
26. Li D., Zhu H., Liu K., Liu X., Leggewie G., Udvardi M., Wang D. Purple acid phosphatases of Arabidopsis thaliana. J. Biol. Chem. 277:2002;27772-27781.
27. Majerus P.W. Inositol phosphate biochemistry. Ann. Rev. Biochem. 61:1992;225-250.
28. McLachlan K.D., Elliott D.E., De Marco D.G., Garran J.H. Leaf acid phosphatase isozymes in the diagnosis of phosphorus status in field-grown wheat. Aust. J. Agric. Res. 38:1987;1-13.
29. Meneguzzo S., Navari-Izzo F., Izzo R. Antioxidative responses of shoots and roots of wheat to increasing NaCl concentrations. J. Plant Physiol. 155:1999;274-280.
30. Murphy J., Riley J. A modified single solution for the determination of phosphate in natural waters. Anal. Chim. Acta. 27:1963;31.
31. Nakai K. Protein sorting signals and prediction of subcellular localization. Adv. Protein Chem. 54:2000;277-344.
32. Nakazato H., Okamoto T., Nishikoori M., Washio K., Morita N., Haraguchi K., Thompson G.A. Jr., Okuyama H. The glycosylphosphatidylinositol-anchored phosphatase from Spirodela oligorrhiza is a purple acid phosphatase. Plant Physiol. 118:1998;1015-1020.
33. Patel K., Lockless S., Thomas B., McKnight T.D. Secreted purple acid phosphatase from Arabidopsis thaliana. Plant Physiol. 119:1998;373-375.
34. Plaxton W.C., Carswell M.C. Metabolic aspects of the phosphate starvation response in plants. Lerner H.R. Plant Responses to Environmental Stresses from Photosynthesis to Genomes Reorganization. 1999;349-371 Marcel Dekker, New York.
35. Puntarulo S., Galleano M., Sanchez R.A., Boveris A. Superoxide anion and hydrogen peroxide metabolism in soybean embryonic axes during germination. Biochim. Biophys. Acta. 1074:1991;277-283.
36. Sambrook J., Russell D.W. Molecular Cloning: A Laboratory Manual. 3rd ed. 2001;Cold Spring Harbor Laboratory Press, New York.
37. Schenk G., Ge Y.B., Carrington L.E., Wynne C.J., Searle I.R., Carroll B.J., Hamilton S., de Jersey J. Binuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybean. Arch. Biochem. Biophys. 370:1999;183-189.
38. Schenk G., Guddat L.W., Ge Y., Carrington L.E., Hume D.A., Hamilton S., de Jersey J. Identification of mammalian-like purple acid phosphatases in a wide range of plants. Gene. 250:2000;117-125.
39. Strater N., Klabunde T., Tucker P., Witzel H., Krebs B. Crystal structure of a purple acid phosphatases containing a dinuclear Fe(III)-Zn(II) active site. Science. 268:1995;1489-1492.
40. Sugiura Y., Kawabe H., Tanaka H., Fujimoto S., Ohara A. Purification, enzymatic properties, and active site environment of a novel manganese (III)-containing acid phosphatase. J. Biol. Chem. 256:1981;10664-10670.
41. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
42. Tsang E.W.T., Bowler C., Herouart D., Van Camp W., Villarroel R., Genetello C., Van Montagu M., Inze D. Differential regulation of superoxide dismutases in plants exposed to environmental stress. Plant Cell. 3:1991;783-792.
43. Vogel A., Borchers T., Marcus K., Meyer H.E., Krebs B., Spener F. Heterologous expression and characterization of recombinant purple acid phosphatase from red kidney bean. Arch. Biochem. Biophys. 401:2002;164-172.
44. Wasaki J., Omura M., Osaki M., Ito H., Matsui H., Shinano T., Tadano T. Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (Lupinus albus L.) roots. Soil Sci. Plant Nutr. 45:1999;439-449.