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. 1970 Aug;103(2):286–294. doi: 10.1128/jb.103.2.286-294.1970

Biosynthesis of the Branched-Chain Amino Acids in Yeast: a Trifluoroleucine-Resistant Mutant with Altered Regulation of Leucine Uptake

Howard Bussey a,1, H E Umbarger a
PMCID: PMC248077  PMID: 5432003

Abstract

A trifluoroleucine-resistant mutant of yeast has been isolated that exhibits reduced incorporation of the analogue into protein (15%) of that in the wild type. In the mutant, uptake of the analogue and leucine into the expandable (water-extractable) pool is enhanced, passage from the expandable to the conversion (nonwater-, ethanol-extractable) pool is unaffected, and endogenous synthesis of leucine is normally regulated. Although the leucyl transfer ribonucluic acid (tRNA) synthetase appears normal, and the tRNAleu has wild-type acceptor activities in vitro and in vivo, the level of the mutant trifluoroleucyl tRNA pool is only 2 to 3% of that in the wild type. The data support the idea of a mutation affecting passage between the conversion pool and the site of charging of the analogue. The mutation is dominant and exhibits pleiotropic effects: the first leucine biosynthetic enzyme appears nonrepressible, and the leucine, valine, and tyrosine uptake systems are constitutively elevated (three- to fourfold) in the absence of exogenous amino acids.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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