Europe and America—Myths and confrontations
In: History of European ideas, Band 20, Heft 1-3, S. 615-620
ISSN: 0191-6599
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In: History of European ideas, Band 20, Heft 1-3, S. 615-620
ISSN: 0191-6599
In: History of European ideas, Band 20, Heft 1-3, S. 615-620
ISSN: 0191-6599
In: The European legacy: the official journal of the International Society for the Study of European Ideas (ISSEI), Band 1, Heft 3, S. 999-1003
ISSN: 1470-1316
8 Pags., 9 Figs. ; Three main families of SODs in plants may be distinguished according to the metal in the active center: CuZnSODs, MnSOD, and FeSOD. CuZnSODs have two sub-families localized either in plant cell cytosol or in plastids, the MnSOD family is essentially restricted to mitochondria, and the FeSOD enzyme family has been typically localized into the plastid. Here, we describe, based on a phylogenetic tree and experimental data, the existence of two FeSOD sub-families: a plastidial localized sub-family that is universal to plants, and a cytosolic localized FeSOD sub-family observed in determinate-forming nodule legumes. Anti-cytosolic FeSOD (cyt_FeSOD) antibodies were employed, together with a novel antibody raised against plastidial FeSOD (p_FeSOD). Stress conditions, such as nitrate excess or drought, markedly increased cyt_FeSOD contents in soybean tissues. Also, cyt_FeSOD content and activity increased with age in both soybean and cowpea plants, while the cyt_CuZnSOD isozyme was predominant during early stages. p_FeSOD in leaves decreased with most of the stresses applied, but this isozyme markedly increased with abscisic acid in roots. The great differences observed for p_FeSOD and cyt_FeSOD contents in response to stress and aging in plant tissues reveal distinct functionality and confirm the existence of two immunologically differentiated FeSOD sub-families. The in-gel FeSOD activity patterns showed a good correlation to cyt_FeSOD contents but not to those of p_FeSOD. This indicates that cyt_FeSOD is the main active FeSOD in soybean and cowpea tissues. The diversity of functions associated with the complexity of FeSOD isoenzymes depending of the location is discussed. ; This work was supported by the Spanish MICINN (Grant Nos. AGL2007-64432/AGR and AGL2010-16167) and by the Government of Navarra (Resolución 57/2007). M.G. and L.P. are grateful for fellowships from the Dept. of Innovation of the Government of Navarra, Spain. ; Peer reviewed
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