{"refrec":{"BRefID":329324,"RR":"<b>Lai, L.B.; Bernal-Bayard, P.; Mohannath, G.; Lai, S.M.; Gopalan, V.; Vioque, A.</b> (2011). A functional RNase P protein subunit of bacterial origin in some eukaryotes. <i>Molecular Genetics and Genomics 286(5-6)</i>: 359-369. <a href=\"https://dx.doi.org/10.1007/s00438-011-0651-y\" target=\"_blank\">https://dx.doi.org/10.1007/s00438-011-0651-y</a>","BEntID":322930,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Molecular Genetics and Genomics 286(5-6)</i>: 359-369. <a href=\"https://dx.doi.org/10.1007/s00438-011-0651-y\" target=\"_blank\">https://dx.doi.org/10.1007/s00438-011-0651-y</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Lai, L.B.; Bernal-Bayard, P.; Mohannath, G.; Lai, S.M.; Gopalan, V.; Vioque, A.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Lai, L.B. <i>et al.</i>","Englishabstract":"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 <i>Ostreococcus tauri</i>. We demonstrate that recombinant <i>O. tauri</i> RPP can functionally reconstitute with bacterial RNase P RNAs (RPRs) but not with <i>O. tauri</i> organellar RPRs, despite the latter’s presumed bacterial origins. We also show that <i>O. tauri</i> PRORP, a homolog of <i>Arabidopsis</i> PRORP-1, displays tRNA 5′-processing activity in vitro. 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