{"refrec":{"BRefID":289282,"RR":"<b>Bernal-Bayard, P.; Puerto-Galán, L.; Vioque, A.</b> (2014). RNase P RNA from the recently evolved plastid of <i>Paulinella</i> and from algae. <i>International Journal of Molecular Sciences 15(11)</i>: 20859-20875. <a href=\"https://dx.doi.org/10.3390/ijms151120859\" target=\"_blank\">https://dx.doi.org/10.3390/ijms151120859</a>","BEntID":281319,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>International Journal of Molecular Sciences 15(11)</i>: 20859-20875. <a href=\"https://dx.doi.org/10.3390/ijms151120859\" target=\"_blank\">https://dx.doi.org/10.3390/ijms151120859</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Bernal-Bayard, P.; Puerto-Galán, L.; Vioque, A.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Bernal-Bayard, P. <i>et al.</i>","Englishabstract":"The RNase P RNA catalytic subunit (RPR) encoded in some plastids has been found to be functionally defective. The amoeba Paulinella chromatophora contains an organelle (chromatophore) that is derived from the recent endosymbiotic acquisition of a cyanobacterium, and therefore represents a model of the early steps in the acquisition of plastids. In contrast with plastid RPRs the chromatophore RPR retains functionality similar to the cyanobacterial enzyme. The chromatophore RPR sequence deviates from consensus at some positions but those changes allow optimal activity compared with mutated chromatophore RPR with the consensus sequence. We have analyzed additional RPR sequences identifiable in plastids and have found that it is present in all red algae and in several prasinophyte green algae. 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