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Het OWA, het open archief van het Waterbouwkundig Laboratorium heeft tot doel alle vrij toegankelijke onderzoeksresultaten van dit instituut in digitale vorm aan te bieden. Op die manier wil het de zichtbaarheid, verspreiding en gebruik van deze onderzoeksresultaten, alsook de wetenschappelijke communicatie maximaal bevorderen.

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RNase P RNA from the recently evolved plastid of Paulinella and from algae Bernal-Bayard, P.; Puerto-Galán, L.; Vioque, A. (2014). RNase P RNA from the recently evolved plastid of Paulinella and from algae. International Journal of Molecular Sciences 15(11): 20859-20875. https://dx.doi.org/10.3390/ijms151120859 In: International Journal of Molecular Sciences. MDPI AG: Basel. ISSN 1661-6596; e-ISSN 1422-0067, meer

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Beschikbaar in	Auteurs
VLIZ: Open access 307060 [ download pdf ]

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Trefwoorden

Exploitable Scientific Result Marine Sciences Marine Sciences > Marine Genomics Scientific Community Scientific Publication Marien/Kust

Author keywords

chloroplast evolution; chromatophore; cyanobacteria; RNase P; tRNAprocessing

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Association of European marine biological laboratories, meer

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Auteurs		Top
Bernal-Bayard, P. Puerto-Galán, L. Vioque, A.

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Abstract

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. We have assayed in vitro a subset of the plastid RPRs not previously analyzed and confirm that these organelle RPRs lack RNase P activity in vitro.

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