SPECIFIC INDUCTION OF CATABOLISM AND ITS RELATION TO REPRESSION OF BIOSYNTHESIS IN ARGININE METABOLISM OF SACCHAROMYCES-CEREVISIAE
SPECIFIC INDUCTION OF CATABOLISM AND ITS RELATION TO REPRESSION OF BIOSYNTHESIS IN ARGININE METABOLISM OF SACCHAROMYCES-CEREVISIAE
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DOI:
10.1016/0022-2836(78)90417-5
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发表时间:
1978-01-01
影响因子:
5.6
通讯作者:
WIAME, JM
中科院分区:
文献类型:
--
作者:
DUBOIS, E;HIERNAUX, D;WIAME, JM
Experimental results are presented in support of the model previously proposed for specific induction of the synthesis of enzymes for arginine catabolism in S. cerevisiae, and its connection with end-product repression of arginine biosynthetic enzymes. The data support the occurrence of negative regulation of metabolism in a eukaryote. Operator regions, one for arginase and another for ornithine transaminase, are identified. The operator mutations are fully constitutive. A mutation compatible with the occurrence of a catabolic repressor, CARGR, leads to partial pleiotropic constitutivity. The connection between the induction process and the repression of biosynthetic enzymes is due to a common receptor of metabolic signals, an ambivalent repressor ARGR endowed with the property of a usual repressor for anabolic enzymes and playing the role of inducer at the level of CARGR; this cascade process simulates a positive control. argR- mutations, by producing defective ARGR, turn on anabolic enzyme synthesis and turn off the synthesis of catabolic enzymes. The dual role of ARGR is confirmed by the isolation of a mutation argRIId which, in contrast to the defective properties caused by usual argR- mutations, causes a dominant hyperactivity toward induction of a catabolic enzyme, but retains recessive hypoactivity toward repression of an anabolic enzyme. Such an ambivalent repressor is a function necessary for mutual, balanced exclusion between opposite metabolisms. Many operator constitutive mutations for arginase, cargA+0-, change the level of enzyme to a similar value, thus defining a genetic function. One of these mutations, cargA+0h, in addition to having unusual genetic behavior, leads to production of twice as much arginase as cargA+0-. This suggests that existence of another genetic region near the structural gene for this enzyme and an additional regulatory function to be analyzed in a separate paper.