Lysine metabolism in antisense C-hordein barley grains

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  • Daiana Schmidt, Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Brazil
  • Vanessa Rizzi, Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Brazil
  • Salete A Gaziola, Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Brazil
  • Leonardo O Medici, Departamento de Ciências Fisiológicas, Universidade Federal Rural do Rio de Janeiro, Brazil
  • Éva Vincze
  • Marcin Kozak, Department of Botany, Warsaw University of Life Sciences, Poland
  • Peter J Lea, Lancaster Environment Centre, University of Lancaster, United Kingdom
  • Ricardo A Azevedo, Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Brazil
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 α-ketoglutarate reductase and saccharopine dehydrogenase were also altered, although the extent varied among the transgenic lines.
Original languageEnglish
JournalPlant Physiology and Biochemistry
Volume87
Pages (from-to)73-83
Number of pages11
ISSN0981-9428
DOIs
Publication statusPublished - 2015

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