Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase

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 cha...

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Detalles Bibliográficos
Autores: Potter, Bastiaan de, Vallee, Ingrid, Camacho, Noelia, Costa Póvoas, Luís Filipe, Bonsembiante, Aureliano, Pons-Pons, Alba, Eckhard, Ulrich, Gomis-Rüth, F. Xavier, Yang, Xiang-Lei, Schimmel, Paul, Kuhle, Bernhard, Pouplana, Lluís Ribas de
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/351039
Acceso en línea:http://hdl.handle.net/10261/351039
Access Level:acceso abierto
Descripción
Sumario: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.

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