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A proteomics study of the induction of somatic embryogenesis in Medicago truncatula using 2DE and MALDI‐TOF/TOF

Identifieur interne : 001562 ( Main/Exploration ); précédent : 001561; suivant : 001563

A proteomics study of the induction of somatic embryogenesis in Medicago truncatula using 2DE and MALDI‐TOF/TOF

Auteurs : André M. Almeida [Portugal] ; José R. Parreira [Portugal] ; Romana Santos [Portugal] ; Ana Sofia Duque [Portugal] ; Rita Francisco [Portugal] ; Daniel F. A. Tomé [Portugal] ; Cândido Pinto Ricardo [Portugal] ; Ana Varela Coelho [Portugal] ; Pedro Fevereiro [Portugal]

Source :

RBID : ISTEX:80BF17773BE5FC561CBADB178EF6D8D7DF716518

Abstract

Medicago truncatula is a model legume, whose genome is currently being sequenced. Somatic embryogenesis (SE) is a genotype‐dependent character and not yet fully understood. In this study, a proteomic approach was used to compare the induction and expression phases of SE of both the highly embryogenic line M9‐10a of M. truncatula cv. Jemalong and its non‐embryogenic predecessor line, M9. The statistical analysis between the lines revealed 136 proteins with significant differential expression (P < 0.05). Of these, 5 had a presence/absence pattern in M9 vs M9‐10a and 22 showed an at least twofold difference in terms of spot volume, were considered of particular relevance to the SE process and therefore chosen for identification. Spots were excised in gel digested with trypsin and proteins were identified using matrix‐assisted laser desorption ionization‐time of flight/time of flight. Identified proteins indicated a higher adaptability of the embryogenic line toward the stress imposed by the inducing culture conditions. Also, some proteins were shown to have a dual pattern of expression: peroxidase, pyrophosphatase and aspartate aminotransferase. These proteins showed higher expression during the induction phases of the M9 line, whereas in the embryogenic line had higher expression at stages coinciding with embryo formation.

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DOI: 10.1111/j.1399-3054.2012.01633.x


Affiliations:


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