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Lysine Transport in Two Barley Mutants with Altered Uptake of Basic Amino Acids in the Root
Simon W. J. Bright, Joseph S. H. Kueh and Sven E. Rognes
Vol. 72, No. 3 (Jul., 1983), pp. 821-824
Published by: American Society of Plant Biologists (ASPB)
Stable URL: http://www.jstor.org/stable/4268120
Page Count: 4
You can always find the topics here!Topics: Plants, Amino acids, Plant roots, Barley, Basic amino acids, Plant cells, Acidic amino acids, Leaves, Cultured cells, Mesophyll cells
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Amino acid uptake was examined in two barley (Hordeum vulgare L.) mutants R906 and R4402 which had been selected as resistant to the lysine analog S-(2-aminoethyl)-cysteine. The mutants were found to be allelic by crossing and examination of F1 and F2 progeny. The mutant genes were designated aec1a and aec1b, respectively. The uptake of the basic amino acids lysine, arginine, and ornithine from 50 micromolar solutions was strongly decreased in roots of the mutants, whereas uptake of neutral and acidic amino acids was unaffected. The pattern of uptake of lysine over the range 10-7 to 10-2 molar was consistent with there being, principally, two uptake systems operating for basic amino acids in roots and that a low-concentration, high-affinity system is reduced or lacking in the mutants. The residual transport activity in the mutants had a different relative affinity for lysine and arginine to the wild-type system. Uptake of lysine by leaf slices was unimpaired in the mutants suggesting that the leaf uptake system is unaffected by the aec1 gene.
Plant Physiology © 1983 American Society of Plant Biologists (ASPB)