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http://hdl.handle.net/2445/208320
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DC Field | Value | Language |
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dc.contributor.author | Potter, Bastiaan de Potter, | - |
dc.contributor.author | Vallee, Ingrid | - |
dc.contributor.author | Camacho, Noelia | - |
dc.contributor.author | Costa Póvoas, Luís Filipe | - |
dc.contributor.author | Bonsembiante, Aureliano | - |
dc.contributor.author | Pons I Pons, Alba | - |
dc.contributor.author | Eckhard, Ulrich | - |
dc.contributor.author | Gomis Rüth, Francesc-Xavier | - |
dc.contributor.author | Yang, Xiang-Lei | - |
dc.contributor.author | Schimmel, Paul | - |
dc.contributor.author | Kuhle, Bernhard | - |
dc.contributor.author | Ribas de Pouplana, Lluís | - |
dc.date.accessioned | 2024-03-03T18:19:16Z | - |
dc.date.available | 2024-03-03T18:19:16Z | - |
dc.date.issued | 2023-08-28 | - |
dc.identifier.issn | 1362-4962 | - |
dc.identifier.uri | http://hdl.handle.net/2445/208320 | - |
dc.description.abstract | Through their aminoacylation reactions, aminoacyl tRNA-synthetases (aaRS) establish the rules of the genetic code throughout all of nature. During their long evolution in eukaryotes, additional domains and splice variants were added to what is commonly a homodimeric or monomeric structure. These changes confer orthogonal functions in cellular activities that have recently been uncovered. An unusual exception to the familiar architecture of aaRSs is the heterodimeric metazoan mitochondrial SerRS. In contrast to domain additions or alternative splicing, here we show that heterodimeric metazoan mitochondrial SerRS arose from its homodimeric ancestor not by domain additions, but rather by collapse of an entire domain (in one subunit) and an active site ablation (in the other). The collapse/ablation retains aminoacylation activity while creating a new surface, which is necessary for its orthogonal function. The results highlight a new paradigm for repurposing a member of the ancient tRNA synthetase family.© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research. | - |
dc.format.extent | 10 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Oxford University Press (OUP) | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1093/nar/gkad696 | - |
dc.relation.ispartof | Nucleic Acids Research, 2023, vol. 51, num. 18, p. 10001-10010 | - |
dc.relation.uri | https://doi.org/10.1093/nar/gkad696 | - |
dc.rights | cc by (c) de Potter, Bastiaan et al., 2023 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.source | Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona)) | - |
dc.subject.classification | RNA | - |
dc.subject.classification | Enzims | - |
dc.subject.other | RNA | - |
dc.subject.other | Enzymes | - |
dc.title | Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.date.updated | 2024-03-01T13:28:27Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.idimarina | 6601966 | - |
dc.identifier.pmid | 37638745 | - |
Appears in Collections: | Articles publicats en revistes (Institut de Recerca Biomèdica (IRB Barcelona)) |
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File | Description | Size | Format | |
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NAR_Ribas_2023.pdf | 1.4 MB | Adobe PDF | View/Open |
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