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Identification and molecular characterization of a low acid phosphatase 3 (lap3) mutant based on the screening of an Arabidopsis activation-tagged population

  • Jin, Yong-Mei (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Research Institute for Agriculture and Life Sciences, Seoul National University) ;
  • Won, So-Youn (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Research Institute for Agriculture and Life Sciences, Seoul National University) ;
  • Jeon, Hye-Sung (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Research Institute for Agriculture and Life Sciences, Seoul National University) ;
  • Park, Sang-Ryoung (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Research Institute for Agriculture and Life Sciences, Seoul National University) ;
  • Kim, Min-Kyun (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Research Institute for Agriculture and Life Sciences, Seoul National University)
  • Received : 2010.09.01
  • Accepted : 2010.10.31
  • Published : 2011.01.31

Abstract

A low acid phosphatase 3 (lap3) mutant was identified and characterized from an Arabidopsis activation-tagged (Weigel) population. The roots of the lap3 plants showed lower acid phosphatase (APase) activity compared to wild-type ones under low-Pi conditions ($10{\mu}M\;Pi$). Plasmid rescue experiments revealed that the activation-tagging vector was inserted into the intergenic region between At4g31540 and At4g31550 in the Arabidopsis genome. The genotypic segregation of the lap3 mutation was tightly linked with the phenotypic segregation of root APase activity in the prgeny of lap3. The transcript level of the At4g31520 (SDA1: SEVERE DEPOLYMERIZATION OF ACTIN 1), located 7.4 kb from the CaMV 35S enhancers in the lap3 mutant, was significantly reduced compared to that in the wild type. It was speculated that cellular actin polymerization may be involved in Pi acquisition in higher plants.

Keywords

References

  1. Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254 https://doi.org/10.1016/0003-2697(76)90527-3
  2. Buscemi G, Saracino F, Masnada D, Carbone ML (2000) The Saccharomyces cerevisiae SDA1 gene is required for actin cytoskeleton organization and cell cycle progression. J Cell Sci 113:1199-1211
  3. Chalfun-Junior A, Mes JJ, Mlynarova L, Aarts MG, Angenent GC (2003) Low frequency of T-DNA based activation tagging in Arabidopsis is correlated with methylation of CaMV 35S enhancer sequences. FEBS Lett 555:459-463 https://doi.org/10.1016/S0014-5793(03)01300-0
  4. Chen DL, Delatorre CA, Bakker A, Abel S (2000) Conditional identification of phosphate-starvation-response mutants in Arabidopsis thaliana. Planta 211:13-22 https://doi.org/10.1007/s004250000271
  5. Coello P (2002) Purification and characterization of secreted acid phosphatase in phosphorus-deficient Arabidopsis thaliana. Physiol Plant 116:293-298 https://doi.org/10.1034/j.1399-3054.2002.1160303.x
  6. Duff SMG, Sarath G, Plaxton WC (1994) The role of acid phosphatases in plant phosphorus metabolism. Physiol Plant 90:791-800 https://doi.org/10.1111/j.1399-3054.1994.tb02539.x
  7. Fang Z, Shao C, Meng Y, Wu P, Chen M (2009) Phosphate signaling in Arabidopsis and Oryza sativa. Plant Sci 176:170-180 https://doi.org/10.1016/j.plantsci.2008.09.007
  8. Goldstein AH, Baertlein DA, Danon A (1989) Phosphate starvation stress as an experimental system for molecular analysis. Plant Mol Biol Rep 7:7-16 https://doi.org/10.1007/BF02669241
  9. Govindan B, Bowser R, Novick P (1995) The role of Myo2, a yeast class V myosin, in vesicular transport. J Cell Biol 128:1055-1068 https://doi.org/10.1083/jcb.128.6.1055
  10. Holford ICR (1997) Soil phosphorus: its measurement, and its uptake by plants. Aust J Soil Res 35:227-240 https://doi.org/10.1071/S96047
  11. Ichikawa T, Nakazawa M, Kawashima M, Muto S, Gohda K, Suzuki K, Ishikawa A, Kobayashi H, Yoshizumi T, Tsumoto Y, Tsuhara Y, Iizumi H, Goto Y, Matsui M (2003) Sequence database of 1172 T-DNA insertion sites in Arabidopsis activation-tagging lines that showed phenotypes in T1 generation. Plant J 36:421-429 https://doi.org/10.1046/j.1365-313X.2003.01876.x
  12. Imaizumi R, Sato S, Kameya N, Nakamura I, Nakamura Y, Tabata S, Ayabe S-i, Aoki T (2005) Activation tagging approach in a model legume, Lotus japonicus. J Plant Res 118:391-399 https://doi.org/10.1007/s10265-005-0231-5
  13. Kandasamy MK, McKinney EC, Deal RB, Meagher RB (2005) Arabidopsis ARP7 is an essential actin-related protein required for normal embryogenesis, plant architecture, and floral organ abscission. Plant Physiol 138:2019-2032 https://doi.org/10.1104/pp.105.065326
  14. Lin WY, Lin SI, Chiou TJ (2009) Molecular regulators of phosphate homeostasis in plants. J Exp Bot 60:1427-1438 https://doi.org/10.1093/jxb/ern303
  15. Marsch-Martinez N, Greco R, Van Arkel G, Herrera-Estrella L, Pereira A (2002) Activation tagging using the En-I maize transposon system in Arabidopsis. Plant Physiol 129:1544-1556 https://doi.org/10.1104/pp.003327
  16. Miura K, Rus A, Sharkhuu A, Yokoi S, Karthikeyan AS, Raghothama KG, Baek D, Koo YD, Jin JB, Bressan RA, Yun DJ, Hasegawa PM (2005) The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses. Proc Natl Acad Sci USA 102:7760-7765 https://doi.org/10.1073/pnas.0500778102
  17. Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 15:473-497 https://doi.org/10.1111/j.1399-3054.1962.tb08052.x
  18. Sanchez-Calderon L, Lopez-Bucio J, Chacon-Lopez A, Cruz-Ramirez A, Nieto-Jacobo F, Dubrovsky JG, Herrera-Estrella L (2005) Phosphate starvation induces a determinate developmental program in the roots of Arabidopsis thaliana. Plant Cell Physiol 46:174-184 https://doi.org/10.1093/pcp/pci011
  19. Tadano T, Ozawa K, Sakai H, Osaki M, Matsui H (1993) Secretion of acid phosphatase by the roots of crop plants under phosphorusdeficient conditions and some properties of the enzyme secreted by lupin roots. Plant Soil 155-156:95-98
  20. Tani H, Chen X, Nurmberg P, Grant JJ, SantaMaria M, Chini A, Gilroy E, Birch PRJ, Loake GJ (2004) Activation tagging in plants: a tool for gene discovery. Funct Integr Genom 4:258-266
  21. Tomscha JL, Trull MC, Deikman J, Lynch JP, Guiltinan MJ (2004) Phosphatase under-producer mutants have altered phosphorus relations. Plant Physiol 135:334-345 https://doi.org/10.1104/pp.103.036459
  22. Trull MC, Deikman J (1998) An Arabidopsis mutant missing one acid phosphatase isoform. Planta 206:544-550 https://doi.org/10.1007/s004250050431
  23. van der Fits L, Hilliou F, Memelink J (2001) T-DNA activation tagging as a tool to isolate regulators of a metabolic pathway from a genetically non-tractable plant species. Transgenic Res 10:513-521 https://doi.org/10.1023/A:1013087011562
  24. Weigel D, Ahn JH, Blazquez MA, Borevitz JO, Christensen SK, Fankhauser C, Ferrandiz C, Kardailsky I, Malancharuvil EJ, Neff MM, Nguyen JT, Sato S, Wang Z-Y, Xia Y, Dixon RA, Harrison MJ, Lamb CJ, Yanofsky MF, Chory J (2000) Activation tagging in Arabidopsis. Plant Physiol 122:1003-1014 https://doi.org/10.1104/pp.122.4.1003
  25. Xu Y, Deng M, Peng J, Hu Z, Bao L, Wang J, Zheng ZL (2010) OsPIE1, the rice ortholog of Arabidopsis photoperiod-independent early flowering 1, is essential for embryo development. PLoS ONE 5:e11299 https://doi.org/10.1371/journal.pone.0011299
  26. Yen Y, Green PJ (1991) Identification and properties of the major ribonucleases of Arabidopsis thaliana. Plant Physiol 97:1487-1493 https://doi.org/10.1104/pp.97.4.1487