An unusual thioredoxin system in the facultative parasite Acanthamoeba castellanii.
Acanthamoeba castellanii
Redox system
Selenoprotein
Thioredoxin reductase
Journal
Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402
Informations de publication
Date de publication:
Apr 2021
Apr 2021
Historique:
received:
30
11
2020
accepted:
02
02
2021
revised:
08
01
2021
pubmed:
19
2
2021
medline:
28
4
2021
entrez:
18
2
2021
Statut:
ppublish
Résumé
The free-living amoeba Acanthamoeba castellanii occurs worldwide in soil and water and feeds on bacteria and other microorganisms. It is, however, also a facultative parasite and can cause serious infections in humans. The annotated genome of A. castellanii (strain Neff) suggests the presence of two different thioredoxin reductases (TrxR), of which one is of the small bacterial type and the other of the large vertebrate type. This combination is highly unusual. Similar to vertebrate TrxRases, the gene coding for the large TrxR in A. castellanii contains a UGA stop codon at the C-terminal active site, suggesting the presence of selenocysteine. We characterized the thioredoxin system in A. castellanii in conjunction with glutathione reductase (GR), to obtain a more complete understanding of the redox system in A. castellanii and the roles of its components in the response to oxidative stress. Both TrxRases localize to the cytoplasm, whereas GR localizes to the cytoplasm and the large organelle fraction. We could only identify one thioredoxin (Trx-1) to be indeed reduced by one of the TrxRases, i.e., by the small TrxR. This thioredoxin, in turn, could reduce one of the two peroxiredoxins tested and also methionine sulfoxide reductase A (MsrA). Upon exposure to hydrogen peroxide and diamide, only the small TrxR was upregulated in expression at the mRNA and protein levels, but not the large TrxR. Our results show that the small TrxR is involved in the A. castellanii's response to oxidative stress. The role of the large TrxR, however, remains elusive.
Identifiants
pubmed: 33599799
doi: 10.1007/s00018-021-03786-x
pii: 10.1007/s00018-021-03786-x
pmc: PMC8038987
doi:
Substances chimiques
Antioxidants
0
Thioredoxins
52500-60-4
Glutathione Reductase
EC 1.8.1.7
Thioredoxin-Disulfide Reductase
EC 1.8.1.9
Glutathione Disulfide
ULW86O013H
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3673-3689Subventions
Organisme : Austrian Science Fund FWF
ID : P 30239
Pays : Austria
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