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SLO2, a mitochondrial pentatricopeptide repeat protein affecting several RNA editing sites, is required for energy metabolism

Qiang Zhu UGent, Jasper Dugardeyn UGent, Chunji Zhang, Mizuki Takenaka, Kristina Kühn, Christian Craddock, Jan Smalle, Michael Karampelias, Jurgen Denecke and Janny Peters, et al. (2012) PLANT JOURNAL. 71(5). p.836-849
abstract
Pentatricopeptide repeat (PPR) proteins belong to a family of approximately 450 members in Arabidopsis, of which few have been characterized. We identified loss of function alleles of SLO2, defective in a PPR protein belonging to the E+ subclass of the P-L-S subfamily. slo2 mutants are characterized by retarded leaf emergence, restricted root growth, and late flowering. This phenotype is enhanced in the absence of sucrose, suggesting a defect in energy metabolism. The slo2 growth retardation phenotypes are largely suppressed by supplying sugars or increasing light dosage or the concentration of CO2. The SLO2 protein is localized in mitochondria. We identified four RNA editing defects and reduced editing at three sites in slo2 mutants. The resulting amino acid changes occur in four mitochondrial proteins belonging to complex I of the electron transport chain. Both the abundance and activity of complex I are highly reduced in the slo2 mutants, as well as the abundance of complexes III and IV. Moreover, ATP, NAD+, and sugar contents were much lower in the mutants. In contrast, the abundance of alternative oxidase was significantly enhanced. We propose that SLO2 is required for carbon energy balance in Arabidopsis by maintaining the abundance and/or activity of complexes I, III, and IV of the mitochondrial electron transport chain.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
PPR PROTEIN, PLANT-MITOCHONDRIA, GENE-EXPRESSION, NICOTIANA-SYLVESTRIS, COMPLEX-I, ARABIDOPSIS-THALIANA, C-OXIDASE DEFICIENCY, RNA editing, pentatricopeptide repeat, mitochondrial electron transport chain, Arabidopsis thaliana, mitochondria, growth retardation, ESCHERICHIA-COLI, RESPIRATORY-CHAIN, MULTIPLE SITES
journal title
PLANT JOURNAL
Plant J.
volume
71
issue
5
pages
836 - 849
Web of Science type
Article
Web of Science id
000307940600012
JCR category
PLANT SCIENCES
JCR impact factor
6.582 (2012)
JCR rank
7/193 (2012)
JCR quartile
1 (2012)
ISSN
0960-7412
DOI
10.1111/j.1365-313X.2012.05036.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2999943
handle
http://hdl.handle.net/1854/LU-2999943
date created
2012-09-27 10:01:46
date last changed
2013-10-02 09:57:20
@article{2999943,
  abstract     = {Pentatricopeptide repeat (PPR) proteins belong to a family of approximately 450 members in Arabidopsis, of which few have been characterized. We identified loss of function alleles of SLO2, defective in a PPR protein belonging to the E+ subclass of the P-L-S subfamily. slo2 mutants are characterized by retarded leaf emergence, restricted root growth, and late flowering. This phenotype is enhanced in the absence of sucrose, suggesting a defect in energy metabolism. The slo2 growth retardation phenotypes are largely suppressed by supplying sugars or increasing light dosage or the concentration of CO2. The SLO2 protein is localized in mitochondria. We identified four RNA editing defects and reduced editing at three sites in slo2 mutants. The resulting amino acid changes occur in four mitochondrial proteins belonging to complex I of the electron transport chain. Both the abundance and activity of complex I are highly reduced in the slo2 mutants, as well as the abundance of complexes III and IV. Moreover, ATP, NAD+, and sugar contents were much lower in the mutants. In contrast, the abundance of alternative oxidase was significantly enhanced. We propose that SLO2 is required for carbon energy balance in Arabidopsis by maintaining the abundance and/or activity of complexes I, III, and IV of the mitochondrial electron transport chain.},
  author       = {Zhu, Qiang and Dugardeyn, Jasper and Zhang, Chunji and Takenaka, Mizuki and K{\"u}hn, Kristina and Craddock, Christian and Smalle, Jan and Karampelias, Michael and Denecke, Jurgen and Peters, Janny and Gerats, Tom and Brennicke, Axel and Eastmond, Peter and Meyer, Etienne H and Van Der Straeten, Dominique},
  issn         = {0960-7412},
  journal      = {PLANT JOURNAL},
  keyword      = {PPR PROTEIN,PLANT-MITOCHONDRIA,GENE-EXPRESSION,NICOTIANA-SYLVESTRIS,COMPLEX-I,ARABIDOPSIS-THALIANA,C-OXIDASE DEFICIENCY,RNA editing,pentatricopeptide repeat,mitochondrial electron transport chain,Arabidopsis thaliana,mitochondria,growth retardation,ESCHERICHIA-COLI,RESPIRATORY-CHAIN,MULTIPLE SITES},
  language     = {eng},
  number       = {5},
  pages        = {836--849},
  title        = {SLO2, a mitochondrial pentatricopeptide repeat protein affecting several RNA editing sites, is required for energy metabolism},
  url          = {http://dx.doi.org/10.1111/j.1365-313X.2012.05036.x},
  volume       = {71},
  year         = {2012},
}

Chicago
Zhu, Qiang, Jasper Dugardeyn, Chunji Zhang, Mizuki Takenaka, Kristina Kühn, Christian Craddock, Jan Smalle, et al. 2012. “SLO2, a Mitochondrial Pentatricopeptide Repeat Protein Affecting Several RNA Editing Sites, Is Required for Energy Metabolism.” Plant Journal 71 (5): 836–849.
APA
Zhu, Q., Dugardeyn, J., Zhang, C., Takenaka, M., Kühn, K., Craddock, C., Smalle, J., et al. (2012). SLO2, a mitochondrial pentatricopeptide repeat protein affecting several RNA editing sites, is required for energy metabolism. PLANT JOURNAL, 71(5), 836–849.
Vancouver
1.
Zhu Q, Dugardeyn J, Zhang C, Takenaka M, Kühn K, Craddock C, et al. SLO2, a mitochondrial pentatricopeptide repeat protein affecting several RNA editing sites, is required for energy metabolism. PLANT JOURNAL. 2012;71(5):836–49.
MLA
Zhu, Qiang, Jasper Dugardeyn, Chunji Zhang, et al. “SLO2, a Mitochondrial Pentatricopeptide Repeat Protein Affecting Several RNA Editing Sites, Is Required for Energy Metabolism.” PLANT JOURNAL 71.5 (2012): 836–849. Print.