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Proteasomal degradation of a trypanosomal ornithine decarboxylase

Nasizadeh, Sima LU ; Jeppsson, A and Persson, Lo LU (2003) In Cellular Physiology and Biochemistry 13(5). p.321-328
Abstract
Mammalian ornithine decarboxylase (ODC), which catalyses the first step in polyamine biosynthesis, has a very fast turnover. It is degraded by the 26S proteasome in an ubiquitin-independent process and the degradation is stimulated by polyamines in a feedback control of the enzyme. Interestingly, there is a major difference in the metabolic stability between ODCs from various trypanosomatids. Trypanosoma brucei and Leishmania donovani both contain stable ODCs, whereas Crithidia fasciculata has an ODC with a rapid turnover. In spite of the difference in stability there is a high degree of sequence homology between C. fasciculata ODC and L. donovani ODC. In the present study we demonstrate that C. fasciculata ODC is rapidly degraded also in... (More)
Mammalian ornithine decarboxylase (ODC), which catalyses the first step in polyamine biosynthesis, has a very fast turnover. It is degraded by the 26S proteasome in an ubiquitin-independent process and the degradation is stimulated by polyamines in a feedback control of the enzyme. Interestingly, there is a major difference in the metabolic stability between ODCs from various trypanosomatids. Trypanosoma brucei and Leishmania donovani both contain stable ODCs, whereas Crithidia fasciculata has an ODC with a rapid turnover. In spite of the difference in stability there is a high degree of sequence homology between C. fasciculata ODC and L. donovani ODC. In the present study we demonstrate that C. fasciculata ODC is rapidly degraded also in mammalian systems like CHO cells and rabbit reticulocyte lysate, suggesting that the degradation signals of the enzyme are recognised by the mammalian systems. L. donovani ODC, on the other hand, is degraded very slowly in the same systems. The degradation of C. fasciculata ODC in the mammalian systems is markedly reduced by inhibition of the 26S proteasome. However, unlike mammalian ODC, C. fasciculata ODC is not downregulated by polyamines. Thus, the turnover of C. fasciculata ODC and L. donovani ODC in the mammalian systems reflects the degradation of the enzyme in the parasites, making such systems potentially useful as complements to parasitic knockout models for further analysis of the mechanisms involved in the rapid degradation of C. fasciculata ODC. Copyright (C) 2003 S. Karger AG, Basel. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
protein turnover, crithidia fasciculata, 26S proteasome, polyamines
in
Cellular Physiology and Biochemistry
volume
13
issue
5
pages
321 - 328
publisher
Karger
external identifiers
  • wos:000186416600010
  • pmid:14586177
  • scopus:0242322029
ISSN
1015-8987
DOI
10.1159/000074548
language
English
LU publication?
yes
id
9d3be0e5-e41f-4a44-8c51-3977de05b2b1 (old id 296553)
date added to LUP
2007-09-18 15:03:22
date last changed
2018-01-07 09:23:30
@article{9d3be0e5-e41f-4a44-8c51-3977de05b2b1,
  abstract     = {Mammalian ornithine decarboxylase (ODC), which catalyses the first step in polyamine biosynthesis, has a very fast turnover. It is degraded by the 26S proteasome in an ubiquitin-independent process and the degradation is stimulated by polyamines in a feedback control of the enzyme. Interestingly, there is a major difference in the metabolic stability between ODCs from various trypanosomatids. Trypanosoma brucei and Leishmania donovani both contain stable ODCs, whereas Crithidia fasciculata has an ODC with a rapid turnover. In spite of the difference in stability there is a high degree of sequence homology between C. fasciculata ODC and L. donovani ODC. In the present study we demonstrate that C. fasciculata ODC is rapidly degraded also in mammalian systems like CHO cells and rabbit reticulocyte lysate, suggesting that the degradation signals of the enzyme are recognised by the mammalian systems. L. donovani ODC, on the other hand, is degraded very slowly in the same systems. The degradation of C. fasciculata ODC in the mammalian systems is markedly reduced by inhibition of the 26S proteasome. However, unlike mammalian ODC, C. fasciculata ODC is not downregulated by polyamines. Thus, the turnover of C. fasciculata ODC and L. donovani ODC in the mammalian systems reflects the degradation of the enzyme in the parasites, making such systems potentially useful as complements to parasitic knockout models for further analysis of the mechanisms involved in the rapid degradation of C. fasciculata ODC. Copyright (C) 2003 S. Karger AG, Basel.},
  author       = {Nasizadeh, Sima and Jeppsson, A and Persson, Lo},
  issn         = {1015-8987},
  keyword      = {protein turnover,crithidia fasciculata,26S proteasome,polyamines},
  language     = {eng},
  number       = {5},
  pages        = {321--328},
  publisher    = {Karger},
  series       = {Cellular Physiology and Biochemistry},
  title        = {Proteasomal degradation of a trypanosomal ornithine decarboxylase},
  url          = {http://dx.doi.org/10.1159/000074548},
  volume       = {13},
  year         = {2003},
}