Cloning of Antizyme Inhibitor, a Highly Homologous Protein to Ornithine Decarboxylase
Copyright policy )Cloning of Antizyme Inhibitor, a Highly Homologous Protein to Ornithine Decarboxylase
The degradation of ornithine decarboxylase (ODC) catalyzed by the 26 S proteasome is accelerated by antizyme, an ODC inhibitory protein induced by polyamines. Previously, we have found another possible regulatory protein of ODC degradation, antizyme inhibitor. Antizyme inhibitor binds to the antizyme with a higher affinity than that of ODC, releasing ODC from ODC-antizyme complex. We report here the cDNA sequence of rat heart antizyme inhibitor. The deduced sequence of the protein is highly similar to, but distinct from, sequences of ODCs from various species. Antizyme inhibitor contains amino acid residues required for formation of active sites of ODC, but it completely lacks ODC activity. Antizyme inhibitor has no homology with peptide sequence in the mammalian ODC carboxyl terminus, which is needed for rapid turnover of ODC. It inhibits antizyme-dependent ODC degradation, but, unlike ODC, its degradation is not accelerated by antizyme.
Mammals, Proteasome Endopeptidase Complex, Binding Sites, Sequence Homology, Amino Acid, Myocardium, Recombinant Fusion Proteins, Molecular Sequence Data, Gene Expression, Proteins, Ornithine Decarboxylase Inhibitors, Ornithine Decarboxylase, Rats, Open Reading Frames, Protein Biosynthesis, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Enzyme Inhibitors, Peptide Hydrolases
Mammals, Proteasome Endopeptidase Complex, Binding Sites, Sequence Homology, Amino Acid, Myocardium, Recombinant Fusion Proteins, Molecular Sequence Data, Gene Expression, Proteins, Ornithine Decarboxylase Inhibitors, Ornithine Decarboxylase, Rats, Open Reading Frames, Protein Biosynthesis, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Enzyme Inhibitors, Peptide Hydrolases
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