A. Craciun et al., Arabidopsis loss-of-function mutant in the lysine pathway points out complex regulation mechanisms, FEBS LETTER, 487(2), 2000, pp. 234-238
In plants, the amino acids lysine, threonine, methionine and isoleucine hav
e L-aspartate-P-semialdehyde (ASA) as a common precursor in their biosynthe
sis pathways. How this ASA precursor is dispersed among the different pathw
ays remains vague knowledge. The proportional balances of free and/or prote
in-bound lysine, threonine, isoleucine and methionine are a function of pro
tein synthesis, secondary metabolism and plant physiology. Some control poi
nts determining the flux: through the distinct pathways are known, but an a
dequate explanation of how the competing pathways share ASA in a fine-tuned
amino acid biosynthesis network is yet not available. In this article me d
iscuss the influence of lysine biosynthesis on the adjacent pathways of thr
eonine and methionine, We report the finding of an Al Arabidopsis thaliana
dihydrodipicolinate synthase T-DNA insertion mutant displaying lower lysine
synthesis, and, as a result of this, a strongly enhanced synthesis of thre
onine, Consequences of these cross-pathway regulations are discussed. (C) 2
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