Open AccessOn the Nature of argR Mutations in Saccharomyces cerevisiae
Author(s) -
Hoet Philippe P.,
Waime JeanMarie
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03388.x
Subject(s) - aminoacylation , saccharomyces cerevisiae , mutant , citrulline , biochemistry , arginine , chemistry , mutation , wild type , biology , genetics , transfer rna , gene , rna , amino acid
Ornithine, citrulline and homoarginine having a regulatory role on arginine biosynthetic enzymes in wild‐type, but not in argR mutants, do not interfere with aminoacylation of tRNA Arg in vitro or in vivo. The same aminoacylation reaction does not seem to be modified in argR mutations, strengthening the hypothesis of a mutation, involving the apopressor.