A functional RNase P protein subunit of bacterial origin in some eukaryotes
Lai, L.B.; Bernal-Bayard, P.; Mohannath, G.; Lai, S.M.; Gopalan, V.; Vioque, A. (2011). A functional RNase P protein subunit of bacterial origin in some eukaryotes. Molecular Genetics and Genomics 286(5-6): 359-369. https://dx.doi.org/10.1007/s00438-011-0651-y
In: Molecular Genetics and Genomics. Springer-Verlag: Berlin. ISSN 1617-4615; e-ISSN 1617-4623, more
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| Keyword |
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| Author keywords |
RNase P diversity, pre-tRNA processing |
| Authors | | Top |
- Lai, L.B.
- Bernal-Bayard, P.
- Mohannath, G.
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- Lai, S.M.
- Gopalan, V.
- Vioque, A.
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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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