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Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 790247, 9 pages
http://dx.doi.org/10.1155/2010/790247
Research Article

A Novel Negative Fe-Deficiency-Responsive Element and a TGGCA-Type-Like FeRE Control the Expression of FTR1 in Chlamydomonas reinhardtii

1Key Laboratory of Tropical Crop Biotechnology, Ministry of Agriculture, Institute of Tropical Bioscience and Biotechnology, Chinese Academy of Tropical Agricultural Science, Haikou 571101, China
2Department of Biochemistry, Hainan Medical College, Haikou 571101, China
3Umeå Plant Science Center, Umeå University, 901 87 Umeå, Sweden

Received 13 October 2009; Accepted 30 December 2009

Academic Editor: Gopi K. Podila

Copyright © 2010 Xiaowen Fei 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. E. Beutler, A. V. Hoffbrand, and J. D. Cook, “Iron deficiency and overload,” Hematology, vol. 1, pp. 40–61, 2003. View at Google Scholar
  2. C. C. Philpott and O. Protchenko, “Response to iron deprivation in Saccharomyces cerevisiae,” Eukaryotic Cell, vol. 7, no. 1, pp. 20–27, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. L. J. Martins, L. T. Jensen, J. R. Simons, G. L. Keller, and D. R. Winge, “Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae,” Journal of Biological Chemistry, vol. 273, no. 37, pp. 23716–23721, 1998. View at Publisher · View at Google Scholar · View at Scopus
  4. D. Radisky and J. Kaplan, “Regulation of transition metal transport across the yeast plasma membrane,” Journal of Biological Chemistry, vol. 274, no. 8, pp. 4481–4484, 1999. View at Publisher · View at Google Scholar · View at Scopus
  5. C. Askwith, D. Eide, A. Van Ho et al., “The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake,” Cell, vol. 76, no. 2, pp. 403–410, 1994. View at Publisher · View at Google Scholar · View at Scopus
  6. R. Stearman, D. S. Yuan, Y. Yamaguchi-Iwai, R. D. Klausner, and A. Dancis, “A permease-oxidase complex involved in high-affinity iron uptake in yeast,” Science, vol. 271, no. 5255, pp. 1552–1557, 1996. View at Google Scholar · View at Scopus
  7. D. R. Dix, J. T. Bridgham, M. A. Broderius, C. A. Byersdorfer, and D. J. Eide, “The FET4 gene encodes the low affinity Fe(II) transport protein of Saccharomyces cerevisiae,” Journal of Biological Chemistry, vol. 269, no. 42, pp. 26092–26099, 1994. View at Google Scholar · View at Scopus
  8. D. Dix, J. Bridgham, M. Broderius, and D. Eide, “Characterization of the FET4 protein of yeast: evidence for a direct role in the transport of iron,” Journal of Biological Chemistry, vol. 272, no. 18, pp. 11770–11777, 1997. View at Publisher · View at Google Scholar · View at Scopus
  9. R. Hassett, D. R. Dix, D. J. Eide, and D. J. Kosman, “The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saccharomyces cerevisiae,” Biochemical Journal, vol. 351, no. 2, pp. 477–484, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. B. M. Waters and D. J. Eide, “Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen,” Journal of Biological Chemistry, vol. 277, no. 37, pp. 33749–33757, 2002. View at Publisher · View at Google Scholar · View at Scopus
  11. Y. Yamaguchi-Iwai, A. Dancis, and R. D. Klausner, “AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae,” EMBO Journal, vol. 14, no. 6, pp. 1231–1239, 1995. View at Google Scholar · View at Scopus
  12. P. L. Blaiseau, E. Lesuisse, and J. M. Camadro, “Aft2p, a novel iron-regulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast,” Journal of Biological Chemistry, vol. 276, no. 36, pp. 34221–34226, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. J. C. Rutherford, S. Jaron, E. Ray, P. O. Brown, and D. R. Winge, “A second iron-regulatory system in yeast independent of Aft1p,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 25, pp. 14322–14327, 2001. View at Publisher · View at Google Scholar · View at Scopus
  14. J. C. Rutherford and A. J. Bird, “Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells,” Eukaryotic Cell, vol. 3, no. 1, pp. 1–13, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Yamaguchi-Iwai, R. Stearman, A. Dancis, and R. D. Klausner, “Iron-regulated DNA binding by the AFT1 protein controls the iron regulon in yeast,” EMBO Journal, vol. 15, no. 13, pp. 3377–3384, 1996. View at Google Scholar · View at Scopus
  16. Y. Yamaguchi-Iwai, R. Ueta, A. Fukunaka, and R. Sasaki, “Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae,” Journal of Biological Chemistry, vol. 277, no. 21, pp. 18914–18918, 2002. View at Publisher · View at Google Scholar · View at Scopus
  17. J. C. Rutherford, S. Jaron, and D. R. Winge, “Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements,” Journal of Biological Chemistry, vol. 278, no. 30, pp. 27636–27643, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. M. Shakoury-Elizeh, J. Tiedeman, J. Rashford et al., “Transcriptional remodeling in response to iron deprivation in Saccharomyces cerevisiae,” Molecular Biology of the Cell, vol. 15, no. 3, pp. 1233–1243, 2004. View at Publisher · View at Google Scholar · View at Scopus
  19. J. M. De Freitas, J. H. Kim, H. Poynton et al., “Exploratory and confirmatory gene expression profiling of mac1d,” Journal of Biological Chemistry, vol. 279, no. 6, pp. 4450–4458, 2004. View at Publisher · View at Google Scholar · View at Scopus
  20. N. J. Robinson, C. M. Procter, E. L. Connolly, and M. L. Guerinot, “A ferric-chelate reductase for iron uptake from soils,” Nature, vol. 397, no. 6721, pp. 694–697, 1999. View at Publisher · View at Google Scholar · View at Scopus
  21. D. Eide, M. Broderius, J. Fett, and M. L. Guerinot, “A novel iron-regulated metal transporter from plants identified by functional expression in yeast,” Proceedings of the National Academy of Sciences of the United States of America, vol. 93, no. 11, pp. 5624–5628, 1996. View at Publisher · View at Google Scholar · View at Scopus
  22. Y. O. Korshunova, D. Eide, W. G. Clark, M. L. Guerinot, and H. B. Pakrasi, “The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range,” Plant Molecular Biology, vol. 40, no. 1, pp. 37–44, 1999. View at Google Scholar · View at Scopus
  23. G. Vert, J. F. Briat, and C. Curie, “Arabidopsis IRT2 gene encodes a root-periphery iron transporter,” Plant Journal, vol. 26, no. 2, pp. 181–189, 2001. View at Publisher · View at Google Scholar · View at Scopus
  24. J. M. Petit, O. van Wuytswinkel, J. F. Briat, and S. Lobréaux, “Characterization of an iron-dependent regulatory sequence involved in the transcriptional control of AtFer1 and ZmFer1 plant ferritin genes by iron,” Journal of Biological Chemistry, vol. 276, no. 8, pp. 5584–5590, 2001. View at Publisher · View at Google Scholar · View at Scopus
  25. J. Wei and E. C. Theil, “Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean),” Journal of Biological Chemistry, vol. 275, no. 23, pp. 17488–17493, 2000. View at Publisher · View at Google Scholar · View at Scopus
  26. N. Okumura, N. K. Nishizawa, Y. Umehara, and S. Mori, “An iron deficiency-specific cDNA from barley roots having two homologous cysteine-rich MT domains,” Plant Molecular Biology, vol. 17, no. 3, pp. 531–533, 1991. View at Publisher · View at Google Scholar · View at Scopus
  27. N. Okumura, N. K. Nishizawa, Y. Umehara et al., “A dioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare,” Plant Molecular Biology, vol. 25, no. 4, pp. 705–719, 1994. View at Google Scholar · View at Scopus
  28. T. Kobayashi, Y. Nakayama, R. N. Itai et al., “Identification of novel cis-acting elements, IDE1 and IDE2, of the barley IDS2 gene promoter conferring iron-deficiency-inducible, root-specific expression in heterogeneous tobacco plants,” Plant Journal, vol. 36, no. 6, pp. 780–793, 2003. View at Publisher · View at Google Scholar · View at Scopus
  29. H. Q. Ling, P. Bauer, Z. Bereczky, B. Keller, and M. Ganal, “The tomato fer gene encoding a bHLH protein controls iron-uptake responses in roots,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 21, pp. 13938–13943, 2002. View at Publisher · View at Google Scholar · View at Scopus
  30. E. P. Colangelo and M. L. Guerinot, “The essential basic helix-loophelix protein FIT1 is required for the iron deficiency response,” Plant Cell, vol. 16, pp. 3400–3412, 2004. View at Google Scholar
  31. T. Brumbarova and P. Bauer, “Iron-mediated control of the basic helix-loop-helix protein FER, a regulator of iron uptake in tomato,” Plant Physiology, vol. 137, no. 3, pp. 1018–1026, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. H. Y. Wang, M. Klatte, M. Jakoby, H. Baumlein, B. Weisshaar, and P. Bauer, “Iron deficiency-mediated stress regulation of four subgroup IbBHLH genes in Arabidopsis thaliana,” Planta, vol. 226, pp. 897–908, 2007. View at Google Scholar
  33. Y. Yuan, H. Wu, N. Wang et al., “FIT interacts with AtbHLH38 and AtbHLH39 in regulating iron uptake gene expression for iron homeostasis in Arabidopsis,” Cell Research, vol. 18, no. 3, pp. 385–397, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. S. La Fontaine, J. M. Quinn, S. S. Nakamoto et al., “Copper-dependent iron assimilation pathway in the model photosynthetic eukaryote Chlamydomonas reinhardtii,” Eukaryotic Cell, vol. 1, no. 5, pp. 736–757, 2002. View at Publisher · View at Google Scholar · View at Scopus
  35. S. J. Lin, R. A. Pufahl, A. Dancis, T. V. O'Halloran, and V. C. Culotta, “A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport,” Journal of Biological Chemistry, vol. 272, no. 14, pp. 9215–9220, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. A. Herbik, C. Bolling, and T. J. Buckhout, “The involvement of a multicopper oxidase in iron uptake by the green algae Chlamydomonas reinhardtii,” Plant Physiology, vol. 130, no. 4, pp. 2039–2048, 2002. View at Publisher · View at Google Scholar · View at Scopus
  37. P. Rubinelli, S. Siripornadulsil, F. Gao-Rubinelli, and R. T. Sayre, “Cadmium- and iron-stress-inducible gene expression in the green alga Chlamydomonas reinhardtii: evidence for H43 protein function in iron assimilation,” Planta, vol. 215, no. 1, pp. 1–13, 2002. View at Publisher · View at Google Scholar · View at Scopus
  38. X. D. Deng and M. Eriksson, “Two iron-responsive promoter elements control expression of FOX1 in Chlamydomonas reinhardtii,” Eukaryotic Cell, vol. 6, pp. 2163–2167, 2007. View at Google Scholar
  39. X. Fei and X. Deng, “A novel Fe deficiency-responsive element (FeRE) regulates the expression of atx1 in Chlamydomonas reinharditii,” Plant and Cell Physiology, vol. 48, no. 10, pp. 1496–1503, 2007. View at Publisher · View at Google Scholar · View at Scopus
  40. X. W. Fei, M. Eriksson, J. H. Yang, and X. D. Deng, “A Fe deficiency responsive element (FeREs) with a core sequence of TGGCA regulates the expression of FEA1 in Chlamydomonas reinharditii,” Journal of Biochemistry, vol. 146, pp. 157–166, 2009. View at Google Scholar
  41. E. H. Harris, The Chlamydomonas Source Book: A Comprehensive Guide to Biology and Laboratory Use, Academic Press, San Diego, Calif, USA, 1989.
  42. J. P. Davies, D. P. Weeks, and A. R. Grossman, “Expression of the arylsulfatase gene from the β 2-tubulin promoter in Chlamydomonas reinhardtii,” Nucleic Acids Research, vol. 20, no. 12, pp. 2959–2965, 1992. View at Google Scholar · View at Scopus
  43. K. L. Kindle, “High frequency nuclear transformation of Chlamydomonas reinhardtii,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, pp. 1228–1232, 1990. View at Google Scholar
  44. R. Debuchy, S. Purton, and J. D. Rochaix, “The argininosuccinate lyase gene of Chlamydomonas reinhardtii: an important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus,” EMBO Journal, vol. 8, no. 10, pp. 2803–2809, 1989. View at Google Scholar · View at Scopus
  45. E. L. De Hostos, R. K. Togasaki, and A. Grossman, “Purification and biosynthesis of a derepressible periplasmic arylsulfatase from Chlamydomonas reinhardtii,” Journal of Cell Biology, vol. 106, no. 1, pp. 29–37, 1988. View at Google Scholar · View at Scopus
  46. K. J. Livak and T. D. Schmittgen, “Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method,” Methods, vol. 25, pp. 402–408, 2001. View at Google Scholar
  47. K. Kucho, S. Yoshioka, F. Taniguchi, K. Ohyama, and H. Fukuzawa, “Cis-acting elements and DNA-binding proteins involved in CO2-responsive transcriptional activation of Cah1 encoding a periplasmic carbonic anhydrase in Chlamydomonas reinhardtii,” Plant Physiology, vol. 133, no. 2, pp. 783–793, 2003. View at Publisher · View at Google Scholar · View at Scopus
  48. J. M. Quinn, P. Barraco, M. Eriksson, and S. Merchant, “Coordinate copper- and oxygen-responsive Cyc6 and Cpx1 expression in Chlamydomonas is mediated by the same element,” Journal of Biological Chemistry, vol. 275, no. 9, pp. 6080–6089, 2000. View at Publisher · View at Google Scholar · View at Scopus
  49. K. Kucho, K. Ohyama, and H. Fukuzawa, “CO2-responsive transcriptional regulation of CAH1 encoding carbonic anhydrase is mediated by enhancer and silencer regions in Chlamydomonas reinhardtii,” Plant Physiology, vol. 121, no. 4, pp. 1329–1337, 1999. View at Google Scholar · View at Scopus
  50. M. Ronen Tarazi, R. Schwarz, A. Bouevitch, J. Lieman-Hurwitz, J. Erez, and A. Kaplan, “Response of photosynthetic microorganisms to changing ambient concentration of CO2,” in Molecular Ecology of Aquatic Microbes, I. Joint, Ed., vol. G38 of NATO ASI Series, pp. 323–334, Springer, Berlin, Germany, 1995. View at Google Scholar