Formation of a ternary complex for selenocysteine biosynthesis in bacteria

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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 [UNESP]
dc.contributor.authorCornelio, Marinonio Lopes [UNESP]
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorThiemann, Otavio Henrique
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2015-12-07T15:38:08Z
dc.date.available2015-12-07T15:38:08Z
dc.date.issued2015-09-16
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.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.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.description.sponsorshipIdFAPESP: 2008/57910-0
dc.description.sponsorshipIdCNPq: 2008/57910-0
dc.description.sponsorshipIdFAPESP: 2010/04429-3
dc.identifierhttp://dx.doi.org/10.1074/jbc.M114.613406
dc.identifier.citationThe Journal Of Biological Chemistry, 2015.
dc.identifier.doi10.1074/jbc.M114.613406
dc.identifier.issn1083-351X
dc.identifier.lattes3874425691257843
dc.identifier.lattes2901888624506535
dc.identifier.pubmed
dc.identifier.urihttp://hdl.handle.net/11449/131587
dc.language.isoeng
dc.publisherThe American Society for Biochemistry and Molecular Biology
dc.relation.ispartofThe Journal Of Biological Chemistry
dc.rights.accessRightsAcesso restrito
dc.sourcePubMed
dc.subjectRna-protein interactionen
dc.subjectBacteriaen
dc.subjectProtein complexen
dc.subjectSelenocysteineen
dc.subjectTransfer RNA (tRNA)en
dc.titleFormation of a ternary complex for selenocysteine biosynthesis in bacteriaen
dc.typeArtigo
dcterms.rightsHolderCopyright © 2015, The American Society for Biochemistry and Molecular Biology.Copyright © 2015, The American Society For Biochemistry And Molecular Biology.
unesp.author.lattes3874425691257843
unesp.author.lattes2901888624506535
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Rio Claropt
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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Artigos - Física - IBILCE
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