Proteomic analysis of mature barley grains from C-hordein antisense lines

Autor(es)

Schmidt, Daiana ^[1] ; Gaziola, Salete Aparecida ^[1] ; Boaretto, Luis Felipe ^[1] ; Azevedo, Ricardo Antunes ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13418900 Piracicaba, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Phytochemistry; v. 125, p. 14-26, MAY 2016.
• Citações Web of Science: 5

Resumo

Hordeins are the major storage proteins in barley grains and are responsible for their low nutritional quality. Previously, antisense C-hordein barley lines were generated and were shown to contain a more balanced amino acid composition and an altered storage protein profile. In the present study, a proteomic approach that combined two-dimensional gel electrophoresis (2-DE) and mass spectrometry was used to (1) identify the changes in the protein profile of non-storage proteins (salt soluble fraction) in antisense C-hordein barley lines (L1, L2 and L3) and (2) map the differentially expressed proteins compared to the non-transgenic control line (Hordeum vulgare cv. Golden Promise). Moreover, the changes in the proteins were correlated with the more balanced amino acid composition of these lines, with special attention to the lysine content. The results showed that suppression of C-hordein expression does not exclusively affect hordein synthesis and accumulation. The more balanced amino acid composition observed in the transgenic lines L1, L2 and L3 was an indirect result of the profound alterations in the patterns of the non-storage proteins. The observed changes included up-regulated expression of the proteins involved in stress and detoxification (L1), defence (L2 and 13), and storage globulins (L1, L2 and L3). To a lesser extent, the proteins involved in grain metabolism were also changed. Thus, the increased essential amino acids content results from changes in distinct protein sources among the three antisense C-hordein lines analyzed, although the up-regulated expression of lysine-rich proteins was consistently observed in all lines. (C) 2016 Elsevier Ltd. All rights reserved. (AU)

• Processo FAPESP: 11/21123-8 - Entendendo o metabolismo de lisina em milho de alta qualidade protéica (QPM) e em cevada geneticamente modificada
• Beneficiário: Daiana Schmidt
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 09/54110-6 - Caracterizacao de enzimas chaves do metabolismo de lisina em cevada (hordeum vulgare l) e em milho (zea mays l.) geneticamente modificados
• Beneficiário: Ricardo Antunes de Azevedo
• Modalidade de apoio: Auxílio à Pesquisa - Regular