Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellualr degradation

L. Ghoda, M. A. Phillips, K. E. Bass, C. C. Wang, P. Coffino

Research output: Contribution to journalArticle

114 Scopus citations

Abstract

Ornithine decarboxylase (ODC) is a key enzyme in polyamine biosynthesis. Mouse ODC is rapidly degraded in mouse cells, whereas ODC within Trypanosoma brucei, a protozoan parasite infesting cattle, is stable. We have expressed cloned ODC genes of both T. brucei and mouse in ODC-deficient Chinese hamster ovary (CHO) cells. The T. brucei enzyme is stable, whereas the mouse ODC similarly expressed in CHO cells is unstable. This shows that the observed difference in intracellular stability is a property of the ODC protein itself, rather than the cellular environment in which it is expressed. A chimeric ODC composed of the amino terminus of trypanosome and the carboxyl terminus of mouse ODC is rapidly degraded in CHO cells, suggesting that peptide sequenes in the mouse ODC carboxyl terminus determine its stability.

Original languageEnglish (US)
Pages (from-to)11823-11826
Number of pages4
JournalJournal of Biological Chemistry
Volume265
Issue number20
StatePublished - Aug 3 1990

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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