Artículo
A functional RNase P protein subunit of bacterial origin in some eukaryotes
Autor/es | Lai, Lien B.
Bernal Bayard, Pilar Mohannath, Gireesha Lai, Stella M. Gopalan, Venkat Vioque Peña, Agustín |
Departamento | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Fecha de publicación | 2011 |
Fecha de depósito | 2019-03-22 |
Publicado en |
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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 ... 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 5′-processing activity in vitro. We discuss the implications of the striking diversity of RNase P in O. tauri, the smallest known free-living eukaryote. |
Identificador del proyecto | BFU2007-60651
P06-CVI-01692 227799 MCB-0238233 MCB-0843543 |
Cita | Lai, L.B., Bernal Bayard, P., Mohannath, G., Lai, S.M., Gopalan, V. y Vioque Peña, A. (2011). A functional RNase P protein subunit of bacterial origin in some eukaryotes. Molecular Genetics and Genomics, 286 (5-6), 359-369. |
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