Increased lysine synthesis in tobacco plants that express high levels of bacterial dihydrodipicolinate synthase in their chloroplasts

Increased lysine synthesis in tobacco plants that express high levels of bacterial... A major nutritional drawback of many crop plants is their low content of several essential amino acids, particularly lysine. The biosynthesis of lysine in plants is regulated by several feedback loops. Dihydrodipicolinate synthase (DHPS) from Escherichia coli, a key enzyme in lysine biosynthesis, which is considerably less sensitive to lysine accumulation than the endogenous plant enzyme has been expressed in chloroplasts of tobacco leaves. Expression of the bacterial enzyme was accompanied by a significant increase in the level of free lysine. No increase in protein‐bound lysine was evident. Free lysine accumulation was positively correlated with the level of DHPS activity in various transgenic plants. Compartmentalization of DHPS in the chloroplast was essential for its participation in lysine biosynthesis as no lysine overproduction was obtained in transgenic plants that expressed the bacterial enzyme in the cytoplasm. The elevated level of free lysine in the transgenic plants was sufficient to inhibit, in vivo, a second key enzyme in lysine biosynthesis, namely, aspartate kinase, with no apparent influence on lysine accumulation. The present report not only provides a better understanding of the regulation of lysine biosynthesis in higher plants but also offers a new strategy to improve the production of this essential amino acid. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Plant Journal Wiley

Increased lysine synthesis in tobacco plants that express high levels of bacterial dihydrodipicolinate synthase in their chloroplasts

The Plant Journal, Volume 2 (2) – Jan 1, 1992

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Publisher
Wiley
Copyright
Copyright © 1992 Wiley Subscription Services
ISSN
0960-7412
eISSN
1365-313X
D.O.I.
10.1111/j.1365-313X.1992.00203.x
Publisher site
See Article on Publisher Site

Abstract

A major nutritional drawback of many crop plants is their low content of several essential amino acids, particularly lysine. The biosynthesis of lysine in plants is regulated by several feedback loops. Dihydrodipicolinate synthase (DHPS) from Escherichia coli, a key enzyme in lysine biosynthesis, which is considerably less sensitive to lysine accumulation than the endogenous plant enzyme has been expressed in chloroplasts of tobacco leaves. Expression of the bacterial enzyme was accompanied by a significant increase in the level of free lysine. No increase in protein‐bound lysine was evident. Free lysine accumulation was positively correlated with the level of DHPS activity in various transgenic plants. Compartmentalization of DHPS in the chloroplast was essential for its participation in lysine biosynthesis as no lysine overproduction was obtained in transgenic plants that expressed the bacterial enzyme in the cytoplasm. The elevated level of free lysine in the transgenic plants was sufficient to inhibit, in vivo, a second key enzyme in lysine biosynthesis, namely, aspartate kinase, with no apparent influence on lysine accumulation. The present report not only provides a better understanding of the regulation of lysine biosynthesis in higher plants but also offers a new strategy to improve the production of this essential amino acid.

Journal

The Plant JournalWiley

Published: Jan 1, 1992

References

  • Development of plant promoter expression vectors and their use for analysis of differential activity of nopaline synthase promoter in transformed tobacco cells
    An, G.
  • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    Arnon, D.I.
  • Two genes for threonine accumulation in barley seeds
    Bright, S.W.J.; Kueh, J.S.H.; Franklin, J.; Rognes, S.E.; Miflin, B.J.
  • Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology
    Cohen, G.N.; Saint‐Girons, I.
  • Selection and characterization of feedback‐insensitive tissue culture of maize
    Hibberd, K.A.; Walter, T.; Green, C.E.; Gengenbach, B.G.
  • Lysine overproducer mutants with an altered di‐hydrodipicolinate synthase from protoplast culture of Nicotiana sylvesfris (Spegazzini and Comes)
    Negrutiu, I.; Cattoir‐Reynaerts, A.; Verbruggen, I.; Jacobs, M.

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