You are in the accessibility menu

Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSilva, Ivan Rosa-
dc.contributor.authorSerrao, Vitor Hugo Balasco-
dc.contributor.authorManzine, Livia Regina-
dc.contributor.authorFaim, Livia Maria-
dc.contributor.authorSilva, Marco Tulio Alves da-
dc.contributor.authorMakki, Raphaela-
dc.contributor.authorSaidemberg, Daniel Menezes-
dc.contributor.authorCornelio, Marinonio Lopes-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorThiemann, Otavio Henrique-
dc.identifier.citationThe Journal Of Biological Chemistry, 2015.-
dc.description.abstractThe synthesis of selenocysteine-containing proteins (selenoproteins) involves the interaction of Selenocysteine Synthase (SelA), tRNA (tRNASec), Selenophosphate Synthetase (SelD, SPS), a specific elongation factor (SelB) and a specific mRNA sequence known as SElenocysteine Insertion Sequence (SECIS). Because selenium compounds are highly toxic in the cellular environment, the association of selenium with proteins throughout its metabolism is essential for cell survival. In this study, we demonstrate the interaction of SPS with the SelA-tRNASec complex, resulting in a 1.3 MDa ternary complex of 27.0 ± 0.5 nm in diameter and 4.02 ± 0.05 nm in height. To assemble the ternary complex, SPS undergoes a conformational change. We demonstrated that the glycine-rich N-terminal region of SPS is crucial for the SelA-tRNASec-SPS interaction and selenoprotein biosynthesis, as revealed by functional complementation experiments. Taken together, our results provide new insights into selenoprotein biosynthesis, demonstrating for the first time the formation of the functional ternary SelA-tRNASec-SPS complex. We propose that this complex is necessary for proper selenocysteine synthesis and may be involved in avoiding the cellular toxicity of selenium compounds.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.publisherThe American Society for Biochemistry and Molecular Biology-
dc.subjectRna-protein interactionen
dc.subjectProtein complexen
dc.subjectTransfer RNA (tRNA)en
dc.titleFormation of a ternary complex for selenocysteine biosynthesis in bacteriaen
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUnespUniversidade Estadual Paulista, Departamento de Física, Instituto de Biociências, Letras e Ciências Exatas de São José do Rio Preto-
dc.description.affiliationUnespUniversidade Estadual Paulista, Departamento de Biologia, Instituto de Biociências de Rio Claro-
dc.description.sponsorshipIdFAPESP: 2008/57910-0-
dc.description.sponsorshipIdCNPq: 2008/57910-0-
dc.description.sponsorshipIdFAPESP: 2010/04429-3-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofThe Journal Of Biological Chemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.