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Título: | A functional RNase P protein subunit of bacterial origin in some eukaryotes |
Autor: | Lai, L.B.; Bernal-Bayard, P. CSIC ORCID ; Mohannath, G.; Lai, S.M.; Gopalan, V.; Vioque, Agustín CSIC ORCID | Fecha de publicación: | 2011 | Editor: | Springer Nature | Citación: | Molecular Genetics and Genomics 286: 359- 369 (2011) | Resumen: | RNase P catalyzes 5'-maturation of tRNAs. While bacterial RNase P comprises an RNA catalyst and a protein cofactor, the eukaryotic (nuclear) variant contains an RNA and up to ten proteins, all unrelated to the bacterial protein. Unexpectedly, a nuclear-encoded bacterial RNase P protein (RPP) homolog is found in several prasinophyte algae including Ostreococcus tauri. We demonstrate that recombinant O. tauri RPP can functionally reconstitute with bacterial RNase P RNAs (RPRs) but not with O. tauri organellar RPRs, despite the latter's presumed bacterial origins. We also show that O. tauri PRORP, a homolog of Arabidopsis PRORP-1, displays tRNA 5α-processing activity in vitro. We discuss the implications of the striking diversity of RNase P in O. tauri, the smallest known freeliving eukaryote. © Springer-Verlag 2011. | URI: | http://hdl.handle.net/10261/59493 | DOI: | 10.1007/s00438-011-0651-y | Identificadores: | doi: 10.1007/s00438-011-0651-y issn: 1617-4615 |
Aparece en las colecciones: | (IBVF) Artículos |
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