Carbamyl‐phosphate synthetase domain of the yeast multifunctional protein Ura2 is necessary for aspartate transcarbamylase inhibition by UTP

FEBS Letters

Estevez, Laurence¹  Denis-Duphil, Michèle¹  Antonelli, Richard¹ 

[1] Département de Génie Biochimique, URA-CNRS 544, Institut National des Sciences Appliquées, Complexe scientifique de Rangueil, 31077 Toulouse, France

关键词: Pyrimidine nucleotide;    URA2;    Multifunctional protein;    UTP regulation;    Saccharomyces cerevisiae;    CP;    carbamyl phosphate;    CPSase;    carbamyl-phosphate synthetase EC 6.3.5.5;    ATCase;    aspartate transcarbamylase EC 2.1.3.2;    DHOase;    dihydroorotase EC 3.5.2.3;    CAD;    acronym for the multifunctional protein which catalyzes in mammalian cells the first three steps of the pyrimidine pathway;    i.e. CPSase;    ATCase;    DHOase;    FUR;    fluorouracil resistant;    FUR2;    mutations allelic to URA2;    GATase;    glutamine amidotransferase;    GFP;    green fluorescent protein from Aequorea victoria;    URA2;    gene URA2;    Ura2;    the protein encoded by URA2;   

DOI  :  10.1016/S0014-5793(98)00010-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown