Distinct domains of antizyme required for binding and proteolysis of ornithine decarboxylase.
Distinct domains of antizyme required for binding and proteolysis of ornithine decarboxylase.
复制标题
鸟氨酸脱羧酶的结合和蛋白水解所需的抗酶的不同结构域。
DOI:
10.1128/mcb.14.1.87-92.1994
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发表时间:
1994
影响因子:
5.3
通讯作者:
Coffino,P
中科院分区:
文献类型:
--
作者:
Li,X;Coffino,P
Selective degradation by proteasomes of ornithine decarboxylase, the initial enzyme in polyamine biosynthesis, is mediated by the polyamine-inducible protein antizyme. Antizyme binds to a region near the N terminus of ornithine decarboxylase (X. Li and P. Coffino, Mol. Cell. Biol. 12:3556-3562, 1992). This interaction induces a conformational change in ornithine decarboxylase that exposes its C terminus and inactivates the enzyme (X. Li and P. Coffino, Mol. Cell. Biol. 13:1487-1492, 1993). Here we show that the C-terminal half of antizyme alone can inactivate ornithine decarboxylase and alter its conformation, but it cannot direct degradation of the enzyme, either in vitro or in vivo. A portion of the N-terminal half of antizyme must be present to promote degradation.