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Enzyme Research
Volume 2011 (2011), Article ID 103980, 7 pages
http://dx.doi.org/10.4061/2011/103980
Review Article

Inorganic Phosphate as an Important Regulator of Phosphatases

1Instituto de Microbiologia Professor Paulo de Góes, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
2Laboratório de Bioquímica Celular, Instituto de Bioquímica Medica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
3Instituto Nacional de Ciência e Tecnologia em Biologia Estrutural e Bioimagens, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil

Received 25 February 2011; Accepted 3 May 2011

Academic Editor: Heung Chin Cheng

Copyright © 2011 Claudia Fernanda Dick et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. D. Barford, A. K. Das, and M. P. Egloff, “The structure and mechanism of protein phosphatases: insights into catalysis and regulation,” Annual Review of Biophysics and Biomolecular Structure, vol. 27, pp. 133–164, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  2. P. Cohen, “The structure and regulation of protein phosphatases,” Annual Review of Biochemistry, vol. 58, pp. 453–508, 1989. View at Google Scholar · View at Scopus
  3. S. Shenolikar, “Protein serine/threonine phosphatases—new avenues for cell regulation,” Annual Review of Cell Biology, vol. 10, pp. 55–86, 1994. View at Google Scholar · View at Scopus
  4. B. Tuleva, E. Vasileva-Tonkova, and D. Galabova, “A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity,” FEMS Microbiology Letters, vol. 161, no. 1, pp. 139–144, 1998. View at Publisher · View at Google Scholar · View at Scopus
  5. T. Hunter, “Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling,” Cell, vol. 80, no. 2, pp. 225–236, 1995. View at Google Scholar · View at Scopus
  6. S. Luan, “Protein phosphatases in plants,” Annual Review of Plant Biology, vol. 54, pp. 63–92, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. X. J. Yang and P. M. Finnegan, “Regulation of phosphate starvation responses in higher plants,” Annals of Botany, vol. 105, no. 4, pp. 513–526, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. M. A. Kutuzov and A. V. Andreeva, “Protein Ser/Thr phosphatases of parasitic protozoa,” Molecular and Biochemical Parasitology, vol. 161, no. 2, pp. 81–90, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  9. S. K. Hanks and T. Hunter, “The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification,” FASEB Journal, vol. 9, no. 8, pp. 576–596, 1995. View at Google Scholar · View at Scopus
  10. T. Watanabe, N. Ozaki, K. Iwashita, T. Fujii, and H. Iefuji, “Breeding of wastewater treatment yeasts that accumulate high concentrations of phosphorus,” Applied Microbiology and Biotechnology, vol. 80, no. 2, pp. 331–338, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. S. Wongwisansri and P. J. Laybourn, “Disruption of histone deacetylase gene RPD3 accelerates PHO5 activation kinetics through inappropriate Pho84p recycling,” Eukaryotic Cell, vol. 4, no. 8, pp. 1387–1395, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  12. A. Kornberg, N. N. Rao, and D. Ault-Riché, “Inorganic polyphosphate: a molecule of many functions,” Annual Review of Biochemistry, vol. 68, pp. 89–125, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  13. R. Ghillebert, E. Swinnen, P. De Snijder, B. Smets, and J. Winderickx, “Differential roles for the low-affinity phosphate transporters Pho87 and Pho90 in Saccharomyces cerevisiae,” Biochemical Journal, vol. 434, no. 2, pp. 243–251, 2010. View at Google Scholar
  14. P. Wu, L. Ma, X. Hou et al., “Phosphate starvation triggers distinct alterations of genome expression in arabidopsis roots and leaves,” Plant Physiology, vol. 132, no. 3, pp. 1260–1271, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. M. Lei, C. Zhu, Y. Liu et al., “Ethylene signalling is involved in regulation of phosphate starvation-induced gene expression and production of acid phosphatases and anthocyanin in Arabidopsis,” New Phytologist, vol. 189, no. 4, pp. 1084–1095, 2010. View at Publisher · View at Google Scholar · View at PubMed
  16. C. Auesukaree, T. Homma, H. Tochio, M. Shirakawa, Y. Kaneko, and S. Harashima, “Intracellular phosphate serves as a signal for the regulation of the PHO pathway in Saccharomyces cerevisiae,” Journal of Biological Chemistry, vol. 279, no. 17, pp. 17289–17294, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. C. F. Dick, A. L. A. dos-Santos, A. L. Fonseca-de-Souza, J. Rocha-Ferreira, and J. R. Meyer-Fernandes, “Trypanosoma rangeli: differential expression of ecto-phosphatase activities in response to inorganic phosphate starvation,” Experimental Parasitology, vol. 124, no. 4, pp. 386–393, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  18. A. L. Fonseca-de-Souza, C. F. Dick, A. L. A. dos Santos, F. V. Fonseca, and J. R. Meyer-Fernandes, “Trypanosoma rangeli: a possible role for ecto-phosphatase activity on cell proliferation,” Experimental Parasitology, vol. 122, no. 3, pp. 242–246, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  19. Y. Kaneko, Y. Tamai, A. Toh-e, and Y. Oshimal, “Transcriptional and post-transcriptional control of PHO8 expression by PHO regulatory genes in Saccharomyces cerevisiae,” Molecular and Cellular Biology, vol. 5, no. 1, pp. 248–252, 1985. View at Google Scholar · View at Scopus
  20. Y. Oshima, N. Ogawa, and S. Harashima, “Regulation of phosphatase synthesis in Saccharomyces cerevisiae—a review,” Gene, vol. 179, no. 1, pp. 171–177, 1996. View at Publisher · View at Google Scholar · View at Scopus
  21. B. L. Persson, J. O. Lagerstedt, J. R. Pratt et al., “Regulation of phosphate acquisition in Saccharomyces cerevisiae,” Current Genetics, vol. 43, no. 4, pp. 225–244, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  22. D. D. Wykoff and E. K. O'Shea, “Phosphate transport and sensing in Saccharomyces cerevisiae,” Genetics, vol. 159, no. 4, pp. 1491–1499, 2001. View at Google Scholar · View at Scopus
  23. K. Huang, I. Ferrin-O'Connell, W. Zhang, G. A. Leonard, E. K. O'Shea, and F. Quiocho, “Structure of the Pho85-Pho80 CDK-cyclin complex of the phosphate-responsive signal transduction pathway,” Molecular Cell, vol. 30, no. 4, pp. 614–623, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  24. Y. Oshima, “The phosphatase system in Saccharomyces cerevisiae,” Genes and Genetic Systems, vol. 72, no. 6, pp. 323–334, 1997. View at Publisher · View at Google Scholar · View at Scopus
  25. A. Kaffman, I. Herskowitz, R. Tjian, and E. K. O'Shea, “Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85,” Science, vol. 263, no. 5150, pp. 1153–1156, 1994. View at Google Scholar · View at Scopus
  26. N. Ogawa, K. I. Noguchi, H. Sawai, Y. Yamashita, C. Yompakdee, and Y. Oshima, “Functional somains of Pho81p, an Inhibitor of Pho85p protein kinase, in the transduction pathway of Pi Signals in Saccharomyces cerevisiae,” Molecular and Cellular Biology, vol. 15, no. 2, pp. 997–1004, 1995. View at Google Scholar · View at Scopus
  27. K. R. Schneider, R. L. Smith, and E. K. O'Shea, “Phosphate-regulated inactivation of the kinase PHO80-PHO85 by the CDK inhibitor PHO81,” Science, vol. 266, no. 5182, pp. 122–126, 1994. View at Google Scholar · View at Scopus
  28. J. M. Mouillon and B. L. Persson, “New aspects on phosphate sensing and signalling in Saccharomyces cerevisiae,” FEMS Yeast Research, vol. 6, no. 2, pp. 171–176, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  29. I. Ciereszko, H. Johansson, V. Hurry, and L. A. Kleczkowski, “Phosphate status affects the gene expression, protein content and enzymatic activity of UDP-glucose pyrophosphorylase in wild-type and pho mutants of Arabidopsis,” Planta, vol. 212, no. 4, pp. 598–605, 2001. View at Publisher · View at Google Scholar · View at Scopus
  30. C. A. Ticconi, C. A. Delatorre, and S. Abel, “Attenuation of phosphate starvation responses by phosphite in Arabidopsis,” Plant Physiology, vol. 127, no. 3, pp. 963–972, 2001. View at Publisher · View at Google Scholar · View at Scopus
  31. I. Stenzel, K. Ziethe, J. Schurath, S. C. Hertel, D. Bosse, and M. Köck, “Differential expression of the LePS2 phosphatase gene family in response to phosphate availability, pathogen infection and during development,” Physiologia Plantarum, vol. 118, no. 1, pp. 138–146, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. E. González, R. Solano, V. Rubio, A. Leyva, and J. Paz-Ares, “Phosphate transporter traffic facilitator1 is a plant-specific SEC12-related protein that enables the endoplasmic reticulum exit of a high-affinity phosphate transporter in Arabidopsis,” Plant Cell, vol. 17, no. 12, pp. 3500–3512, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  33. F. Shimano and H. Ashihara, “Effect of long-term phosphate starvation on the levels and metabolism of purine nucleotides in suspension-cultured Catharanthus roseus cells,” Phytochemistry, vol. 67, no. 2, pp. 132–141, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  34. J. C. Baldwin, A. S. Karthikeyan, A. Cao, and K. G. Raghothama, “Biochemical and molecular analysis of LePS2;1: a phosphate starvation induced protein phosphatase gene from tomato,” Planta, vol. 228, no. 2, pp. 273–280, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  35. A. Torriani, “From cell membrane to nucleotides: the phosphate regulon in Escherichia coli,” BioEssays, vol. 12, no. 8, pp. 371–376, 1990. View at Google Scholar · View at Scopus
  36. R. D. Monds, P. D. Newell, J. A. Schwartzman, and G. A. O'Toole, “Conservation of the Pho regulon in Pseudomonas fluorescens Pf0-1,” Applied and Environmental Microbiology, vol. 72, no. 3, pp. 1910–1924, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. M. G. Lamarche, B. L. Wanner, S. Crépin, and J. Harel, “The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis,” FEMS Microbiology Reviews, vol. 32, no. 3, pp. 1–13, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  38. Y. Tasaki, Y. Kamiya, A. Azwan, T. Hara, and T. Joh, “Gene expression during P deficiency in Pholiota nameko: accumulation of mRNAs for two transporters,” Bioscience, Biotechnology and Biochemistry, vol. 66, no. 4, pp. 790–800, 2002. View at Google Scholar · View at Scopus
  39. P. F. de Gouvêa, F. M. Soriani, I. Malavazi et al., “Functional characterization of the Aspergillus fumigatus PHO80 homologue,” Fungal Genetics and Biology, vol. 45, no. 7, pp. 1135–1146, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. R. L. Metzenberg and W. Chia, “Genetic control of phosphorus assimilation in Neurospora crassa: dose-dependent dominance and recessiveness in constitutive mutants,” Genetics, vol. 93, no. 3, pp. 625–643, 1979. View at Google Scholar · View at Scopus
  41. K. Arima, T. Oshima, I. Kubota, N. Nakamura, T. Mizunaga, and A. Toh-e, “The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide,” Nucleic Acids Research, vol. 11, no. 6, pp. 1657–1672, 1983. View at Google Scholar · View at Scopus
  42. K. A. Bostian, J. M. Lemire, L. E. Cannon, and H. O. Halvorson, “In vitro synthesis of repressible yeast acid phosphatase: identification of multiple mRNAs and products,” Proceedings of the National Academy of Sciences of the United States of America, vol. 77, no. 8, pp. 4504–4508, 1980. View at Google Scholar · View at Scopus
  43. E. J. Kennedy, L. Pillus, and G. Ghosh, “Pho5p and newly identified nucleotide pyrophosphatases/phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae,” Eukaryotic Cell, vol. 4, no. 11, pp. 1892–1901, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  44. S. Wongwisansri and P. J. Laybourn, “Disruption of histone deacetylase gene RPD3 accelerates PHO5 activation kinetics through inappropriate Pho84p recycling,” Eukaryotic Cell, vol. 4, no. 8, pp. 1387–1395, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  45. S. Huang and E. O'Shea, “A systematic high-throughput screen of a yeast deletion collection for mutants defective in PHO5 regulation,” Genetics, vol. 169, no. 4, pp. 1859–1871, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  46. Y. Kaneko, N. Hayashi, A. Toh-e, I. Banno, and Y. Oshima, “Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae,” Gene, vol. 58, no. 1, pp. 137–148, 1987. View at Google Scholar · View at Scopus
  47. C. M. L. Janeway, J. E. Murphy, A. Chaidaroglou, and E. R. Kantrowitz, “Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization ajid catalysis,” Biochemistry, vol. 32, no. 6, pp. 1601–1609, 1993. View at Google Scholar
  48. B. R. LeBansky, T. D. McKnight, and L. R. Gritting, “Purification and characterization of a secreted purple phosphatase from soybean suspension cultures,” Plant Physiology, vol. 99, no. 2, pp. 391–395, 1992. View at Google Scholar · View at Scopus
  49. M. Li and T. Tadano, “Comparison of characteristics of acid phosphatases secreted from roots of lupin and tomato,” Soil Science and Plant Nutrition, vol. 42, no. 4, pp. 753–763, 1996. View at Google Scholar · View at Scopus
  50. J. L. Tomscha, M. C. Trull, J. Deikman, J. P. Lynch, and M. J. Guiltinan, “Phosphatase under-producer mutants have altered phosphorus relations,” Plant Physiology, vol. 135, no. 1, pp. 334–345, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  51. D. Li, H. Zhu, K. Liu et al., “Purple acid phosphatases of Arabidopsis thaliana,” Journal of Biological Chemistry, vol. 277, no. 31, pp. 27772–27781, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  52. G. Schenk, L. W. Guddat, Y. Ge et al., “Identification of mammalian-like purple acid phosphatases in a wide range of plants,” Gene, vol. 250, no. 1-2, pp. 117–125, 2000. View at Publisher · View at Google Scholar · View at Scopus
  53. L. W. Guddat, A. S. McAlpine, D. Hume, S. Hamilton, J. de Jersey, and J. L. Martin, “Crystal structure of mammalian purple acid phosphatase,” Structure, vol. 15, no. 7, pp. 757–767, 1999. View at Publisher · View at Google Scholar · View at Scopus
  54. H. Nakazato, T. Okamoto, M. Nishikoori et al., “The glycosylphosphatidylinositol-anchored phosphatase from Spirodela oligorrhiza is a purple acid phosphatase,” Plant Physiology, vol. 118, no. 3, pp. 1015–1020, 1998. View at Google Scholar · View at Scopus
  55. S. S. Miller, J. Liu, D. L. Allan, C. J. Menzhuber, M. Fedorova, and C. P. Vance, “Molecular control of acid phosphatase secretion into the rhizosphere of proteoid roots from phosphorus-stressed white lupin,” Plant Physiology, vol. 127, no. 2, pp. 594–606, 2001. View at Publisher · View at Google Scholar · View at Scopus
  56. T. Waratrujiwong, B. Krebs, F. Spener, and P. Visoottiviseth, “Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center,” FEBS Journal, vol. 273, no. 8, pp. 1649–1659, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  57. G. Schenk, Y. Ge, L. E. Carrington et al., “Binuclear metal centers in plant purple acid phosphatases: Fe-Zn in sweet potato and Fe-Zn in soybean,” Archives of Biochemistry and Biophysics, vol. 370, no. 2, pp. 183–189, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  58. C. Liang, J. Tian, H. M. Lam, B. L. Lim, X. Yan, and H. Liao, “Biochemical and molecular characterization of PvPAP3, a novel purple acid phosphatase isolated from common bean enhancing extracellular ATP utilization,” Plant Physiology, vol. 152, no. 2, pp. 854–865, 2010. View at Publisher · View at Google Scholar · View at PubMed
  59. J. Wasaki, S. Kojima, H. Maruyama, S. Haase, M. Osaki, and E. Kandeler, “Localization of acid phosphatase activities in the roots of white lupin plants grown under phosphorus-deficient conditions,” Soil Science and Plant Nutrition, vol. 54, no. 1, pp. 95–102, 2008. View at Publisher · View at Google Scholar
  60. G. G. Bozzo, K. G. Raghothama, and W. C. Plaxton, “Structural and kinetic properties of a novel purple acid phosphatase from phosphate-starved tomato (Lycopersicon esculentum) cell cultures,” Biochemical Journal, vol. 377, no. 2, pp. 419–428, 2004. View at Publisher · View at Google Scholar · View at PubMed
  61. G. Dionisio, C. K. Madsen, P. B. Holm et al., “Cloning and characterization of purple acid phosphatase phytases from wheat (Triticum aestivum L.), barley (Hordeum vulgare L.), maize (Zea maize L.) and rice (Oryza sativa L.),” Plant Physiology. In press. View at Publisher · View at Google Scholar
  62. D. D. Lefebvre, S. M. G. Duff, C. A. Fife, C. Julien-Inalsingh, and W. C. Plaxton, “Response to phosphate deprivation in Brassica nigra suspension cells,” Plant Physiology, vol. 93, no. 2, pp. 504–511, 1990. View at Google Scholar
  63. H. Yuan and D. Liu, “Signaling components involved in plant responses to phosphate starvation,” Journal of Integrative Plant Biology, vol. 50, no. 7, pp. 849–859, 2008. View at Publisher · View at Google Scholar · View at PubMed
  64. A. Jungk, B. Seeling, and J. Gerke, “Mobilization of different phosphate fractions in the rhizosphere,” Plant and Soil, vol. 155-156, no. 1, pp. 91–94, 1993. View at Publisher · View at Google Scholar
  65. J. Ascencio, “Acid phosphatase as a diagnostic tool,” Communications in Soil Science and Plant Analysis, vol. 25, pp. 1553–1564, 1994. View at Google Scholar
  66. J. C. Baldwin, A. S. Karthikeyan, and K. G. Raghothama, “LEPS2, a phosphorus starvation-induced novel acid phosphatase from tomato,” Plant Physiology, vol. 125, no. 2, pp. 728–737, 2001. View at Publisher · View at Google Scholar
  67. Q. Zhang, C. Wang, J. Tian, K. Li1, and H. Shou, “Identification of rice purple acid phosphatases related to posphate starvation signaling,” Plant Biology, vol. 13, pp. 7–15, 2011. View at Google Scholar
  68. J. R. Meyer-Fernandes, P. M. Dutra, C. O. Rodrigues, J. Saad-Nehme, and A. H. Lopes, “Mg-dependent ecto-ATPase activity in Leishmania tropica,” Archives of Biochemistry and Biophysics, vol. 341, no. 1, pp. 40–46, 1997. View at Publisher · View at Google Scholar · View at Scopus
  69. J. B. De Jesus, A. A. de Sá Pinheiro, A. H. C. S. Lopes, and J. R. Meyer-Fernandes, “An ectonucleotide ATP-diphosphohydrolase activity in Trichomonas vaginalis stimulated by galactose and its possible role in virulence,” Zeitschrift fur Naturforschung—Section C Journal of Biosciences, vol. 57, no. 9-10, pp. 890–896, 2002. View at Google Scholar · View at Scopus
  70. S. A. Gomes, A. L. Fonseca De Souza, B. A. Silva et al., “Trypanosoma rangeli: differential expression of cell surface polypeptides and ecto-phosphatase activity in short and long epimastigote forms,” Experimental Parasitology, vol. 112, no. 4, pp. 253–262, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  71. A. A. de Sá Pinheiro, J. N. Amazonas, F. de Souza Barros et al., “Entamoeba histolytica: an ecto-phosphatase activity regulated by oxidation-reduction reactions,” Experimental Parasitology, vol. 115, no. 4, pp. 352–358, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  72. C. E. Peres-Sampaio, E. E. de Almeida-Amaral, N. L. L. Giarola, and J. R. Meyer-Fernandes, “Leishmania amazonensis: effects of heat shock on ecto-ATPase activity,” Experimental Parasitology, vol. 119, no. 1, pp. 135–143, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  73. A. L. Fonseca-de-Souza, C. F. Dick, A. L. Santos, and J. R. Meyer-Fernandes, “A Mg(2+)-dependent ecto-phosphatase activity on the external surface of Trypanosoma rangeli modulated by exogenous inorganic phosphate,” Acta Tropica, vol. 107, no. 2, pp. 153–158, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  74. E. C. Fernandes, J. R. Meyer-Fernandes, M. A. C. Silva-Neto, and A. E. Vercesi, “Trypanosoma brucei: ecto-phosphatase activity present on the surface of intact procyclic forms,” Zeitschrift fur Naturforschung, vol. 52, no. 5-6, pp. 351–358, 1997. View at Google Scholar · View at Scopus
  75. N. Sacerdoti-Sierra and C. L. Jaffe, “Release of ecto-protein kinases by the protozoan parasite Leishmania major,” Journal of Biological Chemistry, vol. 272, no. 49, pp. 30760–30765, 1997. View at Publisher · View at Google Scholar · View at Scopus
  76. J. R. Meyer-Fernandes, M. A. Da Silva-Neto, M. Dos Santos Soares, E. Fernandas, A. E. Vercesi, and M. M. De Oliveira, “Ecto-phosphatase activities on the cell surface of the amastigote forms of Trypanosoma cruzi,” Zeitschrift fur Naturforschung—Section C Journal of Biosciences, vol. 54, no. 11, pp. 977–984, 1999. View at Google Scholar · View at Scopus
  77. A. Dos Passos Lemos, A. L. Fonseca de Souza, A. A. De Sá Pinheiro, M. De Berrêdo-Pinho, and J. R. Meyer-Fernandes, “Ecto-phosphatase activity on the cell surface of Crithidia deanei,” Zeitschrift fur Naturforschung, vol. 57, no. 5-6, pp. 500–505, 2002. View at Google Scholar · View at Scopus
  78. J. N. Amazonas, D. Cosentino-Gomes, A. Werneck-Lacerda et al., “Giardia lamblia: characterization of ecto-phosphatase activities,” Experimental Parasitology, vol. 121, no. 1, pp. 15–21, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  79. J. B. Bliska, J. E. Galan, and S. Falkow, “Signal transduction in the mammalian cell during bacterial attachment and entry,” Cell, vol. 73, no. 5, pp. 903–920, 1993. View at Publisher · View at Google Scholar · View at Scopus
  80. J. B. Bliska, K. Guan, J. E. Dixon, and S. Falkow, “Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant,” Proceedings of the National Academy of Sciences of the United States of America, vol. 15, no. 4, pp. 1187–1191, 1991. View at Google Scholar · View at Scopus
  81. M. Braibant and J. Content, “The cell surface associated phosphatase activity of Mycobacterium bovis BCG is not regulated by environmental inorganic phosphate,” FEMS Microbiology Letters, vol. 195, no. 2, pp. 121–126, 2001. View at Publisher · View at Google Scholar · View at Scopus
  82. E. Madec, A. Laszkiewicz, A. Iwanicki, M. Obuchowski, and S. Séror, “Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes,” Molecular Microbiology, vol. 46, no. 2, pp. 571–586, 2002. View at Publisher · View at Google Scholar · View at Scopus
  83. W. N. Arnold, L. C. Mann, K. H. Sakai, R. G. Garrison, and P. D. Coleman, “Acid phosphatases of Sporothrix schenckii,” Journal of General Microbiology, vol. 132, no. 12, pp. 3421–3432, 1986. View at Google Scholar · View at Scopus
  84. M. Bernard, I. Mouyna, G. Dubreucq et al., “Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus,” Microbiology, vol. 148, no. 9, pp. 2819–2829, 2002. View at Google Scholar · View at Scopus
  85. L. F. Kneipp, V. F. Palmeira, A. A. S. Pinheiro et al., “Phosphatase activity on the cell wall of Fonsecaea pedrosoi,” Medical Mycology, vol. 41, no. 6, pp. 469–477, 2003. View at Publisher · View at Google Scholar · View at Scopus
  86. L. F. Kneipp, M. L. Rodrigues, C. Holandino et al., “Ecto-phosphatase activity in conidial forms of Fonsecaea pedrosoi is modulated by exogenous phosphate and influences fungal adhesion to mammalian cells,” Microbiology, vol. 150, no. 10, pp. 3355–3362, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  87. I. Collopy-Junior, F. F. Esteves, L. Nimrichter, M. L. Rodrigues, C. S. Alviano, and J. R. Meyer-Fernandes, “An ectophosphatase activity in Cryptococcus neoformans,” FEMS Yeast Research, vol. 6, no. 7, pp. 1010–1017, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  88. T. Kiffer-Moreira, A. A. De Sá Pinheiro, W. S. Alviano et al., “An ectophosphatase activity in Candida parapsilosis influences the interaction of fungi with epithelial cells,” FEMS Yeast Research, vol. 7, no. 4, pp. 621–628, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  89. M. Gottlieb and D. M. Dwyer, “Protozoan parasite of humans: surface membrane with externally disposed acid phosphatase,” Science, vol. 212, no. 4497, pp. 939–941, 1981. View at Google Scholar · View at Scopus
  90. M. Givskov, L. Eberl, and S. Molin, “Responses to nutrient starvation in Pseudomonas putida KT2442: two- dimensional electrophoretic analysis of starvation- and stress-induced proteins,” Journal of Bacteriology, vol. 176, no. 16, pp. 4816–4824, 1994. View at Google Scholar · View at Scopus
  91. K. Leopold, S. Jacobsen, and O. Nybroe, “A phosphate-starvation-inducible outer-membrane protein of Pseudomonas fluorescens Ag1 as an immunological phosphate-starvation marker,” Microbiology, vol. 143, no. 3, pp. 1019–1027, 1997. View at Google Scholar · View at Scopus
  92. N. Ogawa, J. DeRisi, and P. O. Brown, “New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis,” Molecular Biology of the Cell, vol. 11, no. 12, pp. 4309–4321, 2000. View at Google Scholar · View at Scopus
  93. J. C. Del Pozo, I. Allona, V. Rubio et al., “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 Journal, vol. 19, no. 5, pp. 579–589, 1999. View at Publisher · View at Google Scholar · View at Scopus