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RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae

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 t...

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Detalles Bibliográficos
Autores principales: Bernal-Bayard, Pilar, Puerto-Galán, Leonor, Vioque, Agustín
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4264200/
https://www.ncbi.nlm.nih.gov/pubmed/25402646
http://dx.doi.org/10.3390/ijms151120859
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author Bernal-Bayard, Pilar
Puerto-Galán, Leonor
Vioque, Agustín
author_facet Bernal-Bayard, Pilar
Puerto-Galán, Leonor
Vioque, Agustín
author_sort Bernal-Bayard, Pilar
collection PubMed
description 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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spelling pubmed-42642002014-12-12 RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae Bernal-Bayard, Pilar Puerto-Galán, Leonor Vioque, Agustín Int J Mol Sci Article 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. MDPI 2014-11-13 /pmc/articles/PMC4264200/ /pubmed/25402646 http://dx.doi.org/10.3390/ijms151120859 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Bernal-Bayard, Pilar
Puerto-Galán, Leonor
Vioque, Agustín
RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae
title RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae
title_full RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae
title_fullStr RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae
title_full_unstemmed RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae
title_short RNase P RNA from the Recently Evolved Plastid of Paulinella and from Algae
title_sort rnase p rna from the recently evolved plastid of paulinella and from algae
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4264200/
https://www.ncbi.nlm.nih.gov/pubmed/25402646
http://dx.doi.org/10.3390/ijms151120859
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