Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1991 Aug 1;277(Pt 3):683–685. doi: 10.1042/bj2770683

cis-recognition and degradation of ornithine decarboxylase subunits in reticulocyte lysate.

Y Rosenberg-Hasson 1, Z Bercovich 1, C Kahana 1
PMCID: PMC1151297  PMID: 1872804

Abstract

One of the most interesting characteristics of ornithine decarboxylase (ODC) is its extremely short half-life. In a recent study we have demonstrated that deletion of a C-terminal segment converts ODC into a stable protein. In the present study we have extended this observation by testing the degradation of an ODC heterodimer composed of one rapidly degraded wild-type subunit and one stable mutant subunit. Our study was motivated by the possibility of trans-recognition of stable subunits due to their association with labile subunits. Our results demonstrate that such an association did not confer lability upon the stable subunits, not did it stabilize the short-lived subunits.

Full text

PDF
683

Images in this article

683Fig. 1.
on p.683
684Fig. 2.
on p.684
684Fig. 3.
on p.684

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bercovich Z., Rosenberg-Hasson Y., Ciechanover A., Kahana C. Degradation of ornithine decarboxylase in reticulocyte lysate is ATP-dependent but ubiquitin-independent. J Biol Chem. 1989 Sep 25;264(27):15949–15952. [PubMed] [Google Scholar]
  2. Berger F. G., Szymanski P., Read E., Watson G. Androgen-regulated ornithine decarboxylase mRNAs of mouse kidney. J Biol Chem. 1984 Jun 25;259(12):7941–7946. [PubMed] [Google Scholar]
  3. Ciehanover A., Hod Y., Hershko A. A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun. 1978 Apr 28;81(4):1100–1105. doi: 10.1016/0006-291x(78)91249-4. [DOI] [PubMed] [Google Scholar]
  4. Ghoda L., van Daalen Wetters T., Macrae M., Ascherman D., Coffino P. Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation. Science. 1989 Mar 17;243(4897):1493–1495. doi: 10.1126/science.2928784. [DOI] [PubMed] [Google Scholar]
  5. Heller J. S., Fong W. F., Canellakis E. S. Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction. Proc Natl Acad Sci U S A. 1976 Jun;73(6):1858–1862. doi: 10.1073/pnas.73.6.1858. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hölttä E., Pohjanpelto P. Control of ornithine decarboxylase in Chinese hamster ovary cells by polyamines. Translational inhibition of synthesis and acceleration of degradation of the enzyme by putrescine, spermidine, and spermine. J Biol Chem. 1986 Jul 15;261(20):9502–9508. [PubMed] [Google Scholar]
  7. Isomaa V. V., Pajunen A. E., Bardin C. W., Jänne O. A. Ornithine decarboxylase in mouse kidney. Purification, characterization, and radioimmunological determination of the enzyme protein. J Biol Chem. 1983 Jun 10;258(11):6735–6740. [PubMed] [Google Scholar]
  8. Johnson E. S., Gonda D. K., Varshavsky A. cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature. 1990 Jul 19;346(6281):287–291. doi: 10.1038/346287a0. [DOI] [PubMed] [Google Scholar]
  9. Kahana C., Nathans D. Isolation of cloned cDNA encoding mammalian ornithine decarboxylase. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3645–3649. doi: 10.1073/pnas.81.12.3645. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kahana C., Nathans D. Nucleotide sequence of murine ornithine decarboxylase mRNA. Proc Natl Acad Sci U S A. 1985 Mar;82(6):1673–1677. doi: 10.1073/pnas.82.6.1673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kahana C., Nathans D. Translational regulation of mammalian ornithine decarboxylase by polyamines. J Biol Chem. 1985 Dec 15;260(29):15390–15393. [PubMed] [Google Scholar]
  12. Katz A., Kahana C. Transcriptional activation of mammalian ornithine decarboxylase during stimulated growth. Mol Cell Biol. 1987 Jul;7(7):2641–2643. doi: 10.1128/mcb.7.7.2641. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kitani T., Fujisawa H. Purification and some properties of a protein inhibitor (antizyme) of ornithine decarboxylase from rat liver. J Biol Chem. 1984 Aug 25;259(16):10036–10040. [PubMed] [Google Scholar]
  14. Kontula K. K., Torkkeli T. K., Bardin C. W., Jänne O. A. Androgen induction of ornithine decarboxylase mRNA in mouse kidney as studied by complementary DNA. Proc Natl Acad Sci U S A. 1984 Feb;81(3):731–735. doi: 10.1073/pnas.81.3.731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McConlogue L., Gupta M., Wu L., Coffino P. Molecular cloning and expression of the mouse ornithine decarboxylase gene. Proc Natl Acad Sci U S A. 1984 Jan;81(2):540–544. doi: 10.1073/pnas.81.2.540. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Persson L., Holm I., Heby O. Regulation of ornithine decarboxylase mRNA translation by polyamines. Studies using a cell-free system and a cell line with an amplified ornithine decarboxylase gene. J Biol Chem. 1988 Mar 5;263(7):3528–3533. [PubMed] [Google Scholar]
  17. Rosenberg-Hasson Y., Bercovich Z., Ciechanover A., Kahana C. Degradation of ornithine decarboxylase in mammalian cells is ATP dependent but ubiquitin independent. Eur J Biochem. 1989 Nov 6;185(2):469–474. doi: 10.1111/j.1432-1033.1989.tb15138.x. [DOI] [PubMed] [Google Scholar]
  18. Russell D. H., Snyder S. H. Amine synthesis in regenerating rat liver: extremely rapid turnover of ornithine decarboxylase. Mol Pharmacol. 1969 May;5(3):253–262. [PubMed] [Google Scholar]
  19. Staros J. V. N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers. Biochemistry. 1982 Aug 17;21(17):3950–3955. doi: 10.1021/bi00260a008. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES