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Carbamyl‐phosphate synthetase domain of the yeast multifunctional protein Ura2 is necessary for aspartate transcarbamylase inhibition by UTP
Author(s) -
Antonelli Richard,
Estevez Laurence,
Denis-Duphil Michèle
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00010-6
Subject(s) - carbamyl phosphate , aspartate carbamoyltransferase , saccharomyces cerevisiae , biochemistry , pyrimidine metabolism , carbamoyl phosphate synthetase , mutant , enzyme , yeast , biology , chemistry , allosteric regulation , gene , purine
In Saccharomyces cerevisiae , the first two reactions of pyrimidine biosynthesis are catalyzed by the multifunctional protein Ura2 carrying both carbamyl‐phosphate synthetase (CPSase) and aspartate transcarbamylase (ATCase) enzyme activities. In order to study how UTP regulates both of these activities mutant strains were constructed: one strain which expressed the Ura2 protein fused to the green fluorescent protein, and two strains expressed truncated Ura2 proteins. These strains exhibited a phenotype associated with a modified regulation of the pyrimidine pathway. Results presented in this report provide arguments in favor of a single UTP binding site located on the CPSase domain, and support a model in which ATCase activity is inhibited by UTP only when it can interact with the CPSase domain.