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Proteomic characterisation of subclover seed storage proteins during germination
Author(s) -
SahnounAbid Imene,
Recorbet Ghislaine,
Zuber Hélène,
Sommerer Nicolas,
Centeno Delphine,
DumasGaudot Eliane,
SmitiAschi Samira
Publication year - 2009
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.3666
Subject(s) - vicilin , proteome , imbibition , storage protein , biology , seedling , germination , trifolium subterraneum , botany , pasture , biochemistry , agronomy , gene
BACKGROUND: Early seedling development is a critical step in the establishment of subclover ( Trifolium subterraneum ), an economically important and widespread pasture legume. In this study the seed storage proteome of this non‐model species was characterised in mature dry seeds and during imbibition by using two‐dimensional electrophoresis coupled with tandem mass spectrometry. RESULTS: The phenol‐extracted proteome of subclover dry seeds consisted of 97 polypeptide spots displayed within a window of p I 3–10 and molecular mass 10–150 kDa. De novo sequencing coupled with MS BLAST search enabled the confident identification of 61 proteins, which corresponded to 59 7S vicilin‐ and two 11S legumin‐type globulins. The experimental mobility of vicilin isoforms along with peptide mapping indicated that low‐molecular‐mass polypeptides might account for the post‐translational proteolysis of small vicilin subunits according to the model described for those of pea. Analysis of quantitative changes in the seed storage proteome upon imbibition showed that vicilin catabolism according to a site‐specific process was favoured during early seedling growth in T. subterraneum . CONCLUSION: The establishment of a seed proteome map for T. subterraneum pointed to vicilins as dominant proteins in mature seeds whose catabolism features during early seedling growth may be of relevance under environmental conditions. Copyright © 2009 Society of Chemical Industry