Proteasomal degradation of a trypanosomal ornithine decarboxylase

Cellular Physiology and Biochemistry

Volumn 13, Issue 5, 2003, Pages 321-328

  Nasizadeh, Sima ^a   Jeppsson, Annika ^a   Persson, Lo ^a,b  

^a LUND UNIVERSITY   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

26S proteasome; Crithidia fasciculata; Polyamines; Protein turnover

Indexed keywords

ORNITHINE DECARBOXYLASE; POLYAMINE; PROTEASOME; PROTOZOAL PROTEIN;

ANIMAL CELL; ARTICLE; CHO CELL; CRITHIDIA FASCICULATA; DOWN REGULATION; ENZYME DEGRADATION; ENZYME INHIBITION; EXPERIMENTAL MODEL; FEMALE; HUMAN; LEISHMANIA DONOVANI; MAMMAL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; RETICULOCYTE LYSATE; SPECIES DIFFERENCE;

CRITHIDIA FASCICULATA; LEISHMANIA DONOVANI; MAMMALIA; ORYCTOLAGUS CUNICULUS; TRYPANOSOMA; TRYPANOSOMA BRUCEI;

EID: 0242322029     PISSN: 10158987     EISSN: None     Source Type: Journal    
DOI: 10.1159/000074548     Document Type: Article

References (32)

1. Heby O, Persson L: Molecular genetics of polyamine synthesis in eukaryotic cells. Trends Biochem Sci 1990;15:153-158.
2. Pegg AE, Shantz LM, Coleman CS: Ornithine decarboxylase as a target for chemoprevention. J Cell Biochem 1995;58 Suppl:132-138.
3. Coffino P: Regulation of cellular polyamines by antizyme. Nat Rev Mol Cell Biol 2001;2:188-194.
4. Hayashi S, Murakami Y: Rapid and regulated degradation of ornithine decarboxylase. Biochem J 1995;306:1-10.
5. Hayashi S, Murakami Y, Matsufuji S: Ornithine decarboxylase antizyme: A novel type of regulatory protein. Trends Biochem Sci 1996;21:27-30.
6. Murakami Y, Matsufuji S, Hayashi S, Tanahashi N, Tanaka K: Degradation of ornithine decarboxylase by the 26S proteasome. Biochem Biophys Res Commun 2000;267:1-6.
7. Murakami Y, Matsufuji S, Kameji T, Hayashi S, Igarashi K, Tamura T, Tanaka K, Ichihara A: Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 1992;360:597-599.
8. 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;185:469-474.
9. Ivanov IP, Gesteland RF, Atkins JF: Antizyme expression: a subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit. Nucleic Acids Res 2000;28:3185-3196.
10. Matsufuji S, Matsufuji T, Miyazaki Y, Murakami Y, Atkins JF, Gesteland RF, Hayashi S: Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 1995;80:51-60
11. Rom E, Kahana C: Polyamines regulate the expression of ornithine decarboxylase antizyme in vitro by inducing ribosomal frame-shifting. Proc Natl Acad Sci USA 1994;91:3959-3963.
12. 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;243:1493-1495.
13. Rosenberg-Hasson Y, Bercovich Z, Kahana C: Characterization of sequences involved in mediating degradation of ornithine decarboxylase in cells and in reticulocyte lysate. Eur J Biochem 1991;196:647-651.
14. Ghoda L, Phillips MA, Bass KE, Wang CC, Coffino P: Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation. J Biol Chem 1990;265:11823-11826.
15. Ghoda L, Sidney D, Macrae M, Coffino P: Structural elements of ornithine decarboxylase required for intracellular degradation and polyamine-dependent regulation. Mol Cell Biol 1992;12:2178-2185.
16. Phillips MA, Coffino P, Wang CC: Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei. Implications for enzyme turnover and selective difluoromethylornithine inhibition. J Biol Chem 1987;262:8721-8727.
17. Hanson S, Adelman J, Ullman B: Amplification and molecular cloning of the ornithine decarboxylase gene of Leishmania donovani. J Biol Chem 1992;267:2350-2359.
18. Ceriani C, González NS, Algranati ID: Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation. FEBS Lett 1992;301:261-264.
19. Svensson F, Ceriani C, Lövkvist Wallström E, Kockum I, Algranati ID, Heby O, Persson L: Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain. Proc Natl Acad Sci U S A 1997;94:397-402.
20. Grens A, Steglich C, Pilz R, Scheffler IE: Nucleotide sequence of the Chinese hamster ornithine decarboxylase gene. Nucleic Acids Res 1989;17:10497-10497.
21. Pilz RB, Steglich C, Scheffler IE: Molecular and genetic characterization of an ornithine decarboxylase- deficient Chinese hamster cell line. J Biol Chem 1990;265:8880-8886.
22. Hickok NJ, Seppadie;nen PJ, Gunsalus GL, Jänne OA: Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA. DNA 1987;6:179-187.
23. Kozak M: Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Res 1981;9:5233-5262.
24. 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;264:15949-15952.
25. Tsubuki S, Saito Y, Tomioka M, Ito H, Kawashima S: Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J Biochem (Tokyo) 1996;119:572-576.
26. Carrillo C, Cejas S, Cortes M, Ceriani C, Huber A, Gonzalez NS, Algranati ID: Sensitivity of Trypanosomatid Protozoa to DFMO and Metabolic Turnover of Ornithine Decarboxylase. Biochem Biophys Res Commun 2000;279:663-668.
27. Li Z, Zou CB, Yao Y, Hoyt MA, McDonough S, Mackey ZB, Coffino P, Wang CC: An easily dissociated 26 S proteasome catalyzes an essential ubiquitin-mediated protein degradation pathway in Trypanosoma brucei. J Biol Chem 2002;277:15486-15498.
28. Robertson CD: The Leishmania mexicana proteasome. Mol Biochem Parasitol 1999;103:49-60.
29. Voges D, Zwickl P, Baumeister W: The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999;68:1015-1068.
30. Benaroudj N, Tarcsa E, Cascio P, Goldberg AL: The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes. Biochimie 2001;83:311-318.
31. Hua SB, Li X, Coffino P, Wang CC: Rat antizyme inhibits the activity but does not promote the degradation of mouse ornithine decarboxylase in Trypanosoma brucei. J Biol Chem 1995;270:10264-10271.
32. Rogers S, Wells R, Rechsteiner M: Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986;234:364-368.