Abstract
The metabolic control of branched chain amino acid (BCAA) biosynthesis involves allosteric regulation of acetolactate synthase (ALS) by the end-products of the pathway, valine, leucine and isoleucine. We describe here the molecular basis of valine resistance. We cloned and sequenced an ALS gene from the tobacco mutant Valr-1 and found a single basepair substitution relative to the wild-type allele. This mutation causes a serine to leucine change in the amino acid sequence of ALS at position 214. We then mutagenized the wild-type allele of the ALS gene ofArabidopsis and found that it confers valine resistance when introduced into tobacco plants. Taken together, these results suggest that the serine to leucine change at position 214 of ALS is responsible for valine resistance in tobacco.
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Communicated by A. Kondorosi
This paper is dedicated to the memory of Jean-Pierre Bourgin, who died on October 29, 1994, at the age of 50
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Hervieu, F., Vaucheret, H. A single amino acid change in acetolactate synthase confers resistance to valine in tobacco. Molec. Gen. Genet. 251, 220–224 (1996). https://doi.org/10.1007/BF02172921
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DOI: https://doi.org/10.1007/BF02172921