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J Biol Chem, Vol. 274, Issue 37, 26425-26430, September 10, 1999
,, and§
From the The antizyme family consists of closely
homologous proteins believed to regulate cellular polyamine pools.
Antizyme1, the first described, negatively regulates ornithine
decarboxylase, the initial enzyme in the biosynthetic pathway for
polyamines. Antizyme1 targets ornithine decarboxylase for degradation
and inhibits polyamine transport into cells, thereby diminishing
polyamine pools. A polyamine-stimulated ribosomal frameshift is
required for decoding antizyme1 mRNA. Recently, additional novel
conserved members of the antizyme family have been described. We report here the properties of one of these, antizyme2. Antizyme2, like antizyme1, binds to ornithine decarboxylase and inhibits polyamine transport. Using a baculovirus expression system in cultured
Sf21 insect cells, both antizymes were found to accelerate
ornithine decarboxylase degradation. Expression of either antizyme1 or
2 in Sf21 cells also diminished their uptake of the polyamine
spermidine. Both forms of antizyme can therefore function as negative
regulators of polyamine production and transport. However, in contrast
to antizyme1, antizyme2 has negligible ability to stimulate degradation of ornithine decarboxylase in a rabbit reticulocyte lysate.
Department of Microbiology and Immunology,
§ Department of Medicine, University of California, San
Francisco, California 94143-0414
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