Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation.
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.
Ghoda
L
L
Department of Microbiology and Immunology, University of California, San Francisco 94143.
van Daalen Wetters
T
T
Macrae
M
M
Ascherman
D
D
Coffino
P
P
D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D051379:Mice; D009955:Ornithine Decarboxylase / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014162:Transfection
D011994:Recombinant Proteins; D009955:Ornithine Decarboxylase