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Science 17 March 1989:
Vol. 243. no. 4897, pp. 1493 - 1495
DOI: 10.1126/science.2928784
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Articles

Science, Vol 243, Issue 4897, 1493-1495
Copyright © 1989 by American Association for the Advancement of Science

articles

Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation

L Ghoda, T van Daalen Wetters, M Macrae, D Ascherman, and P Coffino

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

Ornithine decarboxylase (ODC) was converted from a protein with a short intracellular half-life in mammalian cells to a stable protein by truncating 37 residues at its carboxyl terminus. Cells expressing wild-type protein lost ODC activity with a half-life of approximately 1 hour. Cells expressing the truncated protein, however, retained full activity for at least 4 hours. Pulse-chase experiments in which immunoprecipitation and gel electrophoresis were used confirmed the stabilizing effect of the truncation. Thus, a carboxyl-terminal domain is responsible for the rapid intracellular degradation of murine ODC.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)