Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase.
Journal
PLoS neglected tropical diseases
ISSN: 1935-2735
Titre abrégé: PLoS Negl Trop Dis
Pays: United States
ID NLM: 101291488
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
21
01
2020
accepted:
03
08
2020
revised:
29
10
2020
pubmed:
6
10
2020
medline:
23
12
2020
entrez:
5
10
2020
Statut:
epublish
Résumé
Eukaryotes from the Excavata superphylum have been used as models to study the evolution of cellular molecular processes. Strikingly, human parasites of the Trypanosomatidae family (T. brucei, T. cruzi and L. major) conserve the complex machinery responsible for selenocysteine biosynthesis and incorporation in selenoproteins (SELENOK/SelK, SELENOT/SelT and SELENOTryp/SelTryp), although these proteins do not seem to be essential for parasite viability under laboratory controlled conditions. Selenophosphate synthetase (SEPHS/SPS) plays an indispensable role in selenium metabolism, being responsible for catalyzing the formation of selenophosphate, the biological selenium donor for selenocysteine synthesis. We solved the crystal structure of the L. major selenophosphate synthetase and confirmed that its dimeric organization is functionally important throughout the domains of life. We also demonstrated its interaction with selenocysteine lyase (SCLY) and showed that it is not present in other stable assemblies involved in the selenocysteine pathway, namely the phosphoseryl-tRNASec kinase (PSTK)-Sec-tRNASec synthase (SEPSECS) complex and the tRNASec-specific elongation factor (eEFSec) complex. Endoplasmic reticulum stress with dithiothreitol (DTT) or tunicamycin upon selenophosphate synthetase ablation in procyclic T. brucei cells led to a growth defect. On the other hand, only DTT presented a negative effect in bloodstream T. brucei expressing selenophosphate synthetase-RNAi. Furthermore, selenoprotein T (SELENOT) was dispensable for both forms of the parasite. Together, our data suggest a role for the T. brucei selenophosphate synthetase in the regulation of the parasite's ER stress response.
Identifiants
pubmed: 33017394
doi: 10.1371/journal.pntd.0008091
pii: PNTD-D-19-02165
pmc: PMC7595633
doi:
Substances chimiques
Protozoan Proteins
0
Selenoproteins
0
Selenocysteine
0CH9049VIS
Phosphotransferases
EC 2.7.-
selenophosphate synthetase
EC 2.7.9.3
Lyases
EC 4.-
selenocysteine lyase
EC 4.4.1.16
Selenium
H6241UJ22B
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0008091Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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