Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorButantan Institute-
Autor(es): dc.contributorLondon School of Hygiene and Tropical Medicine-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversity of Maryland-
Autor(es): dc.contributorUniversidade Federal de São Carlos (UFSCar)-
Autor(es): dc.creatorda Silva, Marco Túlio Alves-
Autor(es): dc.creatorE Silva, Ivan Rosa-
Autor(es): dc.creatorFaim, Lívia Maria-
Autor(es): dc.creatorBellini, Natália Karla-
Autor(es): dc.creatorPereira, Murilo Leão-
Autor(es): dc.creatorLima, Ana Laura-
Autor(es): dc.creatorde Jesus, Teresa Cristina Leandro-
Autor(es): dc.creatorCosta, Fernanda Cristina-
Autor(es): dc.creatorWatanabe, Tatiana Faria [UNESP]-
Autor(es): dc.creatorPereira, Humberto D’Muniz-
Autor(es): dc.creatorValentini, Sandro Roberto [UNESP]-
Autor(es): dc.creatorZanelli, Cleslei Fernando [UNESP]-
Autor(es): dc.creatorBorges, Júlio Cesar-
Autor(es): dc.creatorDias, Marcio Vinicius Bertacine-
Autor(es): dc.creatorda Cunha, Júlia Pinheiro Chagas-
Autor(es): dc.creatorMittra, Bidyottam-
Autor(es): dc.creatorAndrews, Norma W.-
Autor(es): dc.creatorThiemann, Otavio Henrique-
Data de aceite: dc.date.accessioned2022-02-22T00:52:26Z-
Data de disponibilização: dc.date.available2022-02-22T00:52:26Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-10-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1371/journal.pntd.0008091-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/208104-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/208104-
Descrição: dc.descriptionEukaryotes 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, SELE-NOT/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 selenocys-teine 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.-
Descrição: dc.descriptionLaboratory of Structural Biology Sao Carlos Institute of Physics University of São Paulo-
Descrição: dc.descriptionLaboratory of Cell Cycle and Center of Toxins Immune Response and Cell Signaling-CeTICS Butantan Institute-
Descrição: dc.descriptionLondon School of Hygiene and Tropical Medicine-
Descrição: dc.descriptionSchool of Pharmaceutical Sciences São Paulo State University (UNESP)-
Descrição: dc.descriptionSão Carlos Institute of Chemistry University of São Paulo-
Descrição: dc.descriptionDepartment of Microbiology Institute of Biomedical Science University of São Paulo-
Descrição: dc.descriptionDepartment of Cell Biology and Molecular Genetics University of Maryland-
Descrição: dc.descriptionDepartment of Genetics and Evolution Federal University of São Carlos-
Descrição: dc.descriptionSchool of Pharmaceutical Sciences São Paulo State University (UNESP)-
Formato: dc.format1-31-
Idioma: dc.languageen-
Relação: dc.relationPLoS Neglected Tropical Diseases-
???dc.source???: dc.sourceScopus-
Título: dc.titleTrypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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