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Mol Cell Biol. 1994 January; 14(1): 87-92

Distinct domains of antizyme required for binding and proteolysis of ornithine decarboxylase.

X Li and P Coffino

Department of Microbiology and Immunology, University of California, San Francisco 94143.

ABSTRACT

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.

Mol Cell Biol. 1994 January; 14(1): 87-92




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