Lysine metabolism in antisense C-hordein barley grains

Autor(es)

Schmidt, Daiana ^[1] ; Rizzi, Vanessa ^[1] ; Gaziola, Salete A. ^[1] ; Medici, Leonardo O. ^[2] ; Vincze, Eva ^[3] ; Kozak, Marcin ^[4] ; Lea, Peter J. ^[5] ; Azevedo, Ricardo A. ^[1]

Afiliação do(s) autor(es)

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

^[2] Univ Fed Rural Rio de Janeiro, Dept Ciencias Fisiol, BR-23890000 Seropedica - Brazil

^[3] Univ Aarhus, Fac Agr Sci, Res Ctr Flakkebjerg, Dept Genet & Biotechnol, DK-4200 Slagelse - Denmark

^[4] Warsaw Univ Life Sci, SGGW, Dept Bot, PL-02766 Warsaw - Poland

^[5] Univ Lancaster, Lancaster Environm Ctr, Lancaster LA1 4YQ - England

• Tipo de documento: Artigo Científico
• Fonte: Plant Physiology and Biochemistry; v. 87, p. 73-83, FEB 2015.
• Citações Web of Science: 5

Resumo

The grain proteins of barley are deficient in lysine and threonine due to their low concentrations in the major storage protein class, the hordeins, especially in the C-hordein subgroup. Previously produced antisense C-hordein transgenic barley lines have an improved amino acid composition, with increased lysine, methionine and threonine contents. The objective of the study was to investigate the possible changes in the regulation of key enzymes of the aspartate metabolic pathway and the contents of aspartate-derived amino acids in the nontransgenic line (Hordeum vulgare L. cv. Golden Promise) and five antisense C-hordein transgenic barley lines. Considering the amounts of soluble and protein-bound aspartate-derived amino acids together with the analysis of key enzymes of aspartate metabolic pathway, we suggest that the C-hordein suppression did not only alter the metabolism of at least one aspartate-derived amino acid (threonine), but major changes were also detected in the metabolism of lysine and methionine. Modifications in the activities and regulation of aspartate kinase, dihydrodipicolinate synthase and homoserine dehydrogenase were observed in most transgenic lines. Furthermore the activities of lysine a-ketoglutarate reductase and saccharopine dehydrogenase were also altered, although the extent varied among the transgenic lines. (C) 2014 Elsevier Masson SAS. 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: 04/16039-4 - Entendendo o metabolismo de lisina em cereais
• Beneficiário: Ricardo Antunes de Azevedo
• Modalidade de apoio: Auxílio à Pesquisa - Temático