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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Schmidt, Daiana [1] ; Gaziola, Salete Aparecida [1] ; Boaretto, Luis Felipe [1] ; Azevedo, Ricardo Antunes [1]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13418900 Piracicaba, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: Phytochemistry; v. 125, p. 14-26, MAY 2016.
Web of Science Citations: 5
Abstract

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)

FAPESP's process: 11/21123-8 - Understanding the lysine metabolism in quality protein maize (QPM) and in genetic modified barley
Grantee:Daiana Schmidt
Support Opportunities: Scholarships in Brazil - Doctorate