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A functional RNase P protein subunit of bacterial origin in some eukaryotes

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Abstract

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.

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Acknowledgments

We thank Dr. M. L. S. Raj for cloning the tobacco chloroplast pre-tRNAGly(GCC) in pUC19. This work was supported by Ministerio de Ciencia e Innovación, Spain, and European Regional Fund [BFU2007-60651 (to A.V.)], Junta de Andalucía, Spain [P06-CVI-01692 (to A.V.)], European Union [ASSEMBLE grant agreement no. 227799 (to A.V.)], and the National Science Foundation [MCB-0238233 and MCB-0843543 (to V.G.)]. Pilar Bernal-Bayard was supported by a fellowship from Junta de Andalucía, Spain.

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The authors declare they have no conflict of interest.

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Correspondence to Venkat Gopalan or Agustín Vioque.

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Communicated by C. Dieckmann.

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Lai, L.B., Bernal-Bayard, P., Mohannath, G. et al. A functional RNase P protein subunit of bacterial origin in some eukaryotes. Mol Genet Genomics 286, 359–369 (2011). https://doi.org/10.1007/s00438-011-0651-y

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