Summary
Iron-sulfur (Fe-S) clusters are co-factors of proteins that perform a number of biological roles, including electron transfer, redox and non-redox catalysis, regulation of gene expression, and as sensors within all living organisms, prokaryotes and eukaryotes. These clusters are thought to be among the oldest structures found in biological cells. In chloroplasts, Fe-S clusters play a key role in photosynthetic electron transport as well as nitrogen and sulfur assimilation. The capacity of the Fe atom in Fe-S clusters to take up an electron reversibly provides the required electron carrier capacity in these pathways. Iron and sulfur limitation both affect plant primary production and growth. It has long been known that iron deficiency leads to defects in photosynthesis and bleaching in young leaves, phenomena that are closely linked to a defect in chloroplastic photosystem- I (PSI) accumulation, a major Fe-S containing protein complex in plants. Although the functional importance of Fe-S cluster proteins is evident and isolated chloroplasts have been shown to be able to synthesize their own Fe-S clusters, much is yet to be learned about the biosynthesis of Fe-S proteins in plastids. The recent discovery of a NifS-like protein in plastids has hinted to the existence of an assembly machinery related to bacterial Fe-S assembly systems. This chapter aims to summarize what we presently know about the assembly of Fe-S clusters in plants with an emphasis on green plastids.
Access provided by Autonomous University of Puebla. Download to read the full chapter text
Chapter PDF
Similar content being viewed by others
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
Beinert, H., Holm, R.H. and Münck, E. (1997) Science 277, 653–659.
Imsande, J. (1999) Plant Physiol. Biochem. 37, 87–97.
Vorburger Mielcsarek, E. and Bertch McGrayne, S. (2000) Iron, Nature’s Universal Element. Rutgers University Press, New Brunswick, N.J. pp. 1–204.
Lill, R. and Kispal, G. (2000) Trends Biochem. Sci. 25, 352–356.
Frazzon, J., Fick, J.R. and Dean, D.R. (2002) Biochem. Soc. Trans. 30, 680–685.
Raven, J.A., Evans, M.C. and Korb, R.E. (1999) Photosynthesis Res. 60, 111–149.
Lancaster, J.R., Vega, J.M., Kamin, H., Orme-Johnson, N.R., Orme-Johnson, W.H., Krueger, W.H. and Siegel, L.M. (1979) J. Biol. Chem. 254, 1268–1272.
Krueger, R.J. and Siegel, L.M. (1982) Biochemistry 21, 2892–2904.
Munekage, Y., Hashimoto, M., Miyake, C., Tomizawa, K., Endo, T., Tasaka, M. and Shikanai, T. (2004) Nature 429, 579–582.
Marschner, H. (1995) Mineral Nutrition of Higher Plants, Academic Press, London. pp. 3–384.
Chitnis, P.R. (2001) Ann. Rev. Plant Physiol. Plant Mol. Biol. 52, 593–626.
Buchanan, B.B., Gruissem, W.G. and Jones, R.L. (2000) Biochemistry and Molecular Biology of Plants. Amer. Soc. Plant Biol., Rockville, MD. pp. 2–1367.
Kispal, G., Csere, P., Prohl, C. and Lill, R. (1999) EMBO J. 18, 3981–3989.
Kushnir, S., Babiychuk, E., Storozhenko, S., Davey, M.W., Papenbrock, J., De Rycke, R., Engler, G., Stephan, U.W., Lange, H., Kispal, G., Lill, R. and Van Montagu, M. (2001) Plant Cell 13, 89–100.
Balk, J., Pierik, A.J., Netz, D.J., Muhlenhoff, U. and Lill, R (2004) EMBO J. 23, 2105–2115.
Keegstra, K. and Cline, K. (1999) Plant Cell 11, 557–570.
Li, H-M., Theg, S.M., Bauerle, C.M. and Keegstra, K. (1990) Proc. Nat. Acad. Sci. U.S.A. 8, 6748–6752.
Pilon, M., de Kruijff, B. and Weisbeek, P.J. (1992) J. Biol. Chem. 267, 2548–2556.
Pilon, M., America, T., van’t Hof, R., de Kruijff, B. and Weisbeek, P. (1995) Advances in Molecular and Cell Biology (Rothman, S.S. ed.) Membrane Protein Transport. JAI Press, Greenwich, CT. Vol. 4, pp. 229–255.
Merchant, S. and Dreyfuss B.W. (1998) Ann. Rev. Plant Physiol. Plant Mol. Biol. 49, 25–51.
Takahashi, Y., Mitsui, A., Hase, T. and Matsubara, H. (1986) Proc. Nat. Acad. Sci. U.S.A. 83, 2434–2437.
Takahashi, Y., Mitsui, A. and Matsubara, H. (1990) Plant Physiol. 95, 97–103.
Pilon-Smits, E.A.H., Garifullina, G., Abdel-Ghany, S., Kato, S., Mihara, H., Hale, K.L., Burkhead, J., Esaki, N., Kurihara, T. and Pilon, M. (2002) Plant Physiol. 130, 1309–1318.
Leon, S., Touraine, B., Briat, J-F. and Lobreaux, S. (2002) Biochem. J. 366, 557–564.
Curie, C. and Briat, J.F. (2003) Ann. Rev. Plant Physiol. Plant Mol. Biol. 54, 183–206.
Hell, R. and Stephan, U.W. (2003) Planta 216, 541–551.
Curie, C., Panaviene, Z., Loulergue, C., Dellaporta, S.L., Briat, J.F. and Walker, E.L. (2001) Nature 409, 346–349.
Robinson, N.J., Procterm, C.M., Connolly, E.L. and Guerinot M.L. (1999) Nature 397, 694–697.
Connolly, E.L., Fett, J.P. and Guerinot, M.L. (2002) Plant Cell 14, 1347–1357.
Vert, G., Grotz, N., Dedaldechamp, F., Gaymard, F., Guerinot, M.L., Briat, J.F. and Curie, C. (2002) Plant Cell 14, 1223–1233.
Shingles, R., North, M. and McCarty, R.E. (2002) Plant Physiol. 128, 1022–1030.
Petit, J-M., Briat, J-F. and Lobreaux, S. (2001) Biochem. J. 359, 575–582.
Beinert, H. (2000). Eur. J. Biochem. 267, 5657–5664.
Leustek, T., Martin, M.N., Bick, J-A. and Davies, J.P. (2000) Ann. Rev. Plant Physiol. Plant Mol. Biol. 5, 141–165.
Smith, F.W., Ealing, P.M., Hawkesford, M.J. and Clarkson, D.T. (1995) Proc. Nat. Acad. Sci. U.S.A. 92, 9373–9377.
Shibagaki, N., Rose, A., McDermott, J., Fujiwara, T., Hayashi, H., Yoneyama, T. and Davies, J.P. (2002) Plant J. 29, 475–486.
Yoshimoto, N., Takahashi, H., Smith, F.W., Yamaya, T. and Saito, K. (2002) Plant J. 29, 465–473.
Takahashi, H., Yamazaki, M., Sasakura, N., Watanabe, A., Leustek, T., de Almeida Engler, J., van Montagu, M. and Saito, K. (1997) Proc. Nat. Acad. Sci. U.S.A. 94, 1102–11107.
Takahashi, H., Watanabe-Takahashi, A., Smith, F.W., Blake-Kalff, M., Hawkesford, M.J. and Saito, K. (2000) Plant J. 23, 171–182.
Takahashi, H., Sasakura, N., Kimura, A., Watanabe, A. and Saito, K. (1999) Plant Physiol. 121, 686.
Grossman, A.R. and Takahashi, H. (2001) Ann. Rev. Plant Physiol. Plant Mol. Biol. 52, 163–210.
Rotte, C. and Leustek, T. (2000) Plant Physiol. 124, 715–724.
Bork, C., Schwenn, J.D. and Hell, R. (1998) Gene 212, 147–153.
Zhou, J. and Goldsbrough, P.B. (1994) Plant Cell 6, 875–884.
Axelsen, K.B. and Palmgren, M.G. (2001) Plant Physiol. 126, 696–706.
Zheng, L., White, R.H., Cash, V.L., Jack, R.F. and Dean, D.R. (1993) Proc. Nat. Acad. Sci. U.S.A. 90, 2754–2758.
Mihara, H. and Esaki, N. (2002) Appl. Microbiol. Biotechnol. 60, 12–23.
Mihara, H., Kurihara, T., Yoshimura, T., Soda, K. and Esaki, N. (1997) J. Biol. Chem. 272, 22417–22424.
Zheng, L., Cash, V.L., Flint, D.H. and Dean, D.R.(1998) J. Biol. Chem. 273, 13264–13272.
Agar, J.N., Krebs, C., Frazzon, J., Huynh, B.H., Dean, D.R. and Johnson, M.K. (2000) Biochemistry 39, 7856–7862.
Krebs, C., Agar, J.N., Smith, A.D., Frazzon, J., Dean, D.R., Huynh, B.H. and Johnson M.K. (2001) Biochemistry 40, 14069–14080.
Muhlenhoff, U., Gerber, J., Richhardt, N. and Lill, R. (2003) EMBO J. 22, 4815–4825.
Takahashi, Y. and Tokumoto, U. (2002) J. Biol. Chem. 277, 28380–28383.
Nachin, L., Loiseau, L., Expert, D. and Barras, F. (2003) EMBO J. 22, 427–437.
Outten, F.W., Djaman, O. and Storz, G. (2004) Mol. Microbiol. 52, 861–872.
Ollagnier-de Choudens, S., Nachin, L., Sanakis, Y., Loiseau, L., Barras, F. and Fontecave, M. (2003) J. Biol. Chem. 278, 17993–18001.
Loiseau, L., Ollagnier-de-Choudens, S., Nachin, L., Fontecave, M. and Barras, F. (2003) J. Biol. Chem. 278, 38352–38359.
Outten, F.W., Wood, M.J., Munoz, F.M. and Storz, G. (2003) J. Biol. Chem. 278, 45713–45719.
Ye, H., Garifullina, G.F., Abdel-Ghany, S., Zhang, L., Pilon-Smits, E.A.H. and Pilon, M. (2004) Planta 220, 602–608 (2005).
Leon, S., Touraine, B., Ribot, C., Briat, J.F. and Lobreaux, S. (2003) Biochem. J. 371, 823–830.
Yabe, T., Morimoto, K., Kikuchi, S., Nishio, K., Terashima, I. and Nakai, M. (2004) Plant Cell 16, 993–1007.
Touraine, B., Boutin, J-P., Marion Poll, A., Briat, J-F., Peltier, G. and Lobreaux S. (2004) Plant J., 40, 101–111
Møller, G.M., Kunkel, T. and Chua, N.-H. (2001) Genes Dev. 15, 90–103.
Xu, X.M. and Møller, S.G. (2004) Proc. Nat. Acad. Sci. U.S.A. 101, 9143–9148.
Wintz, H., Fox. T., Wu, Y.Y., Feng, V., Chen, W., Chang, H.S., Zhu, T. and Vulpe, C. (2003) J. Biol. Chem. 278, 47644–47653.
Lezhneva, L., Amann, K. and Meurer, J. (2004) Plant J. 37, 174–85.
Noctor, G., Arisi, A.C.M., Jouanin, L. and Foyer, C.H. (1998) Plant Physiol. 118, 471–482.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2006 Springer Science+Business Media, Inc.
About this chapter
Cite this chapter
Pilon, M., Abdel-Ghany, S.E., Van Hoewyk, D., Ye, H., Pilon-Smits, E.A.H. (2006). Biogenesis of Iron-Sulfur Cluster Proteins in Plastids. In: Setlow, J.K. (eds) Genetic Engineering. Genetic Engineering: Principles and Methods, vol 27. Springer, Boston, MA. https://doi.org/10.1007/0-387-25856-6_7
Download citation
DOI: https://doi.org/10.1007/0-387-25856-6_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-25855-3
Online ISBN: 978-0-387-25856-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)