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Title

The GmFAD7 gene family from soybean: identification of novel genes and tissue-specific conformations of the FAD7 enzyme involved in desaturase activity

AuthorsAndreu Gargallo, Vanesa ; Lagunas Castán, Beatriz ; Collados Collados, Raquel; Picorel Castaño, Rafael ; Alfonso Lozano, Miguel
Keywordsdesaturase
FAD7
fatty-acid
gene expression
plastid
protein conformation
soybean
Issue DateJul-2010
PublisherOxford University Press
CitationAndreu V, Lagunas B, Collados R, Picorel R, Alfonso M. The GmFAD7 gene family from soybean: identification of novel genes and tissue-specific conformations of the FAD7 enzyme involved in desaturase activity. Journal of experimental botany 61 (12): 3371-3384 (2010)
AbstractThe FAD7 gene encodes a ω3 fatty acid desaturase which catalyses the production of trienoic fatty acids (TAs) in plant chloroplasts. A novel GmFAD7 gene (named GmFAD7-2) has been identified in soybean, with high homology to the previously annotated GmFAD7 gene. Genomic sequencing analysis together with searches at the soybean genome database further confirmed that both GmFAD7 genes were located in two different loci within the soybean genome, suggesting that the soybean ω3 plastidial desaturase FAD7 is encoded by two different paralogous genes. Both GmFAD7-1 and GmFAD7-2 genes were expressed in all soybean tissues examined, displaying their highest mRNA accumulation in leaves. This expression profile contrasted with GmFAD3A and GmFAD3B mRNA accumulation, which was very low in this tissue. These results suggested a concerted control of plastidial and reticular ω3 desaturase gene expression in soybean mature leaves. Analysis of GmFAD7 protein distribution in different soybean tissues showed that, in mature leaves, two bands were detected, coincident with the higher expression level of both GmFAD7 genes and the highest 18:3 fatty acid accumulation. By contrast, in seeds, where FAD7 activity is low, specific GmFAD7 protein conformations were observed. These GmFAD7 protein conformations were affected in vitro by changes in the redox conditions of thiol groups and iron availability. These results suggest the existence of tissue-specific post-translational regulatory mechanisms affecting the distribution and conformation of the FAD7 enzymes related with the control of its activity.
Description40 Pag., 8 Fig. The definitive version is available at: http://jxb.oxfordjournals.org/
Publisher version (URL)http://dx.doi.org/10.1093/jxb/erq158
URIhttp://hdl.handle.net/10261/42439
DOI10.1093/jxb/erq158
ISSN0022-0957
E-ISSN1460-2431
Appears in Collections:(EEAD) Artículos
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