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Functional analysis of SLO2 provides new insight into the role of plant PPR proteins

PPR (Pentatricopeptide repeat) proteins are mainly involved in RNA metabolism. In Arabidopsis, the PPR family is composed of more than 450 members; however, only few of them were functionally characterized. In a previous report,1 we identified a novel mitochondrial PPR RNA editing factor, named SLO2...

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Detalles Bibliográficos
Autores principales: Zhu, Qiang, H. Meyer, Etienne, Van Der Straeten, Dominique
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3493397/
https://www.ncbi.nlm.nih.gov/pubmed/22902704
http://dx.doi.org/10.4161/psb.21430
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author Zhu, Qiang
H. Meyer, Etienne
Van Der Straeten, Dominique
author_facet Zhu, Qiang
H. Meyer, Etienne
Van Der Straeten, Dominique
author_sort Zhu, Qiang
collection PubMed
description PPR (Pentatricopeptide repeat) proteins are mainly involved in RNA metabolism. In Arabidopsis, the PPR family is composed of more than 450 members; however, only few of them were functionally characterized. In a previous report,1 we identified a novel mitochondrial PPR RNA editing factor, named SLO2, which is responsible for 7 editing events in Arabidopsis. Loss-of-function mutation in SLO2 results in plant growth retardation, and delayed development, and leads to the dysfunction of mitochondrial complex I, III and IV. slo2 is the first example of a single gene mutation affecting 3 complexes of the mitochondrial electron transport chain. This Short Communication discusses the conservation of upstream regions of editing sites affected by SLO2 and illustrates the effect of mutation of SLO2 on activation of the alternative pathway. We also reflect upon the implications and perspectives of these findings.
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spelling pubmed-34933972012-11-16 Functional analysis of SLO2 provides new insight into the role of plant PPR proteins Zhu, Qiang H. Meyer, Etienne Van Der Straeten, Dominique Plant Signal Behav Short Communication PPR (Pentatricopeptide repeat) proteins are mainly involved in RNA metabolism. In Arabidopsis, the PPR family is composed of more than 450 members; however, only few of them were functionally characterized. In a previous report,1 we identified a novel mitochondrial PPR RNA editing factor, named SLO2, which is responsible for 7 editing events in Arabidopsis. Loss-of-function mutation in SLO2 results in plant growth retardation, and delayed development, and leads to the dysfunction of mitochondrial complex I, III and IV. slo2 is the first example of a single gene mutation affecting 3 complexes of the mitochondrial electron transport chain. This Short Communication discusses the conservation of upstream regions of editing sites affected by SLO2 and illustrates the effect of mutation of SLO2 on activation of the alternative pathway. We also reflect upon the implications and perspectives of these findings. Landes Bioscience 2012-10-01 /pmc/articles/PMC3493397/ /pubmed/22902704 http://dx.doi.org/10.4161/psb.21430 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Short Communication
Zhu, Qiang
H. Meyer, Etienne
Van Der Straeten, Dominique
Functional analysis of SLO2 provides new insight into the role of plant PPR proteins
title Functional analysis of SLO2 provides new insight into the role of plant PPR proteins
title_full Functional analysis of SLO2 provides new insight into the role of plant PPR proteins
title_fullStr Functional analysis of SLO2 provides new insight into the role of plant PPR proteins
title_full_unstemmed Functional analysis of SLO2 provides new insight into the role of plant PPR proteins
title_short Functional analysis of SLO2 provides new insight into the role of plant PPR proteins
title_sort functional analysis of slo2 provides new insight into the role of plant ppr proteins
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3493397/
https://www.ncbi.nlm.nih.gov/pubmed/22902704
http://dx.doi.org/10.4161/psb.21430
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