Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization.

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  • dc.contributor.author Mariotti, Marco, 1984-ca
  • dc.contributor.author Santesmasses Ruiz, Didac, 1978-ca
  • dc.contributor.author Capella Gutiérrez, Salvador Jesús, 1985-ca
  • dc.contributor.author Mateo, Andreaca
  • dc.contributor.author Arnan Ros, Carmeca
  • dc.contributor.author Johnson, Roryca
  • dc.contributor.author D’Aniello, Salvatoreca
  • dc.contributor.author Yim, Sun Heeca
  • dc.contributor.author Gladyshev, Vadim N.ca
  • dc.contributor.author Serras Rigalt, Florencica
  • dc.contributor.author Corominas Guiu, Montserratca
  • dc.contributor.author Gabaldón Estevan, Juan Antonio, 1973-ca
  • dc.contributor.author Guigó Serra, Rodericca
  • dc.date.accessioned 2015-10-30T09:36:26Z
  • dc.date.available 2015-10-30T09:36:26Z
  • dc.date.issued 2015
  • dc.description.abstract Selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme Selenophosphate synthetase (SPS or SelD), conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. Here, we study the evolutionary history of SPS genes, providing a map of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologs that replace the Sec site with cysteine (Cys) are common. Many metazoans, however, possess SPS genes with substitutions other than Sec or Cys (collectively referred to as SPS1). Using complementation assays in fly mutants, we show that these genes share a common function, which appears to be distinct from the synthesis of selenophosphate carried out by the Sec- and Cys- SPS genes (termed SPS2), and unrelated to Sec synthesis. We show here that SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. Thus, in SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. This evolutionary history constitutes a remarkable example of emergence and evolution of gene function, which we have been able to trace thanks to the singular features of SPS genes, wherein the amino acid at a single site determines unequivocally protein function and is intertwined to the evolutionary fate of the entire selenoproteome.ca
  • dc.description.sponsorship R.G. group research was funded by grants BIO2011-26205 from the Spanish Ministry of Science and grant SGR-1430 from the Catalan Government. M.M. received a FPU doctoral fellowship AP2008-04334 from the Spanish Ministry of Education. T.G. group research was funded in part by a grant from the Spanish Ministry of Economy and Competitiveness (BIO2012-37161), a grant from the Qatar National Research Fund (Grant No. NPRP 5-298-3-086), and a grant from the European Research Council under the European Union’s Seventh Framework Programme (FP/2007-2013)/ERC (Grant Agreement n. ERC-2012-StG-310325). R.G. and T.G. acknowledge support of the Spanish Ministry of Economy and Competitiveness, “Centro de Excelencia Severo Ochoa 2013-2017,” SEV-2012-0208. V.N.G. group research was supported by the National Institutes of Health (NIH) GM061603.
  • dc.format.mimetype application/pdfca
  • dc.identifier.citation Mariotti M, Santesmasses D, Capella-Gutierrez S, Mateo A, Arnan C, Johnson R. et al. Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization. Genome Res. 2015 Sep;25(9):1256-67. DOI: 10.1101/gr.190538.115.ca
  • dc.identifier.doi http://dx.doi.org/10.1101/gr.190538.115
  • dc.identifier.issn 1088-9051
  • dc.identifier.uri http://hdl.handle.net/10230/24968
  • dc.language.iso engca
  • dc.publisher Cold Spring Harbor Laboratory Pressca
  • dc.relation.ispartof Genome Research. 2015 Sep;25(9):1256-67
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2011-26205
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2012-37161
  • dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/310325
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/SEV2012-0208
  • dc.rights © 2015 Mariotti et al. This article, published in Genome Research, is available/nunder a Creative Commons License (Attribution 4.0 International), as described/nat http://creativecommons.org/licenses/by/4.0/.ca
  • dc.rights.accessRights info:eu-repo/semantics/openAccessca
  • dc.rights.uri http://creativecommons.org/licenses/by/4.0/ca
  • dc.subject.other Proteïnesca
  • dc.subject.other Aminoàcidsca
  • dc.title Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization.ca
  • dc.type info:eu-repo/semantics/articleca
  • dc.type.version info:eu-repo/semantics/publishedVersionca

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