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Multiple PPR protein interactions are involved in the RNA editing system in Arabidopsis mitochondria and plastids

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Abstract
Recent identification of several different types of RNA editing factors in plant organelles suggests complex RNA editosomes within which each factor has a different task. However, the precise protein interactions between the different editing factors are still poorly understood. In this paper, we show that the E+-type pentatricopeptide repeat (PPR) protein SLO2, which lacks a C-terminal cytidine deaminase-like DYW domain, interacts in vivo with the DYW-type PPR protein DYW2 and the P-type PPR protein NUWA in mitochondria, and that the latter enhances the interaction of the former ones. These results may reflect a protein scaffold or complex stabilization role of NUWA between E+-type PPR and DYW2 proteins. Interestingly, DYW2 and NUWA also interact in chloroplasts, and DYW2-GFP overexpressing lines show broad editing defects in both organelles, with predominant specificity for sites edited by E+-type PPR proteins. The latter suggests a coordinated regulation of organellar multiple site editing through DYW2, which probably provides the deaminase activity to E+ editosomes.
Keywords
DYW2, NUWA, PPR, RNA editing, SLO2, PENTATRICOPEPTIDE REPEAT PROTEINS, SUBCELLULAR-LOCALIZATION, PLANT-MITOCHONDRIA, DYW DOMAIN, IDENTIFICATION, RECOGNITION, SITE, PEROXISOMES, MACHINERY, THALIANA

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MLA
Andres Colas, Nuria, et al. “Multiple PPR Protein Interactions Are Involved in the RNA Editing System in Arabidopsis Mitochondria and Plastids.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 114, no. 33, 2017, pp. 8883–88, doi:10.1073/pnas.1705815114.
APA
Andres Colas, N., Zhu, Q., Takenaka, M., De Rybel, B., Weijers, D., & Van Der Straeten, D. (2017). Multiple PPR protein interactions are involved in the RNA editing system in Arabidopsis mitochondria and plastids. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 114(33), 8883–8888. https://doi.org/10.1073/pnas.1705815114
Chicago author-date
Andres Colas, Nuria, Qiang Zhu, Mizuki Takenaka, Bert De Rybel, Dolf Weijers, and Dominique Van Der Straeten. 2017. “Multiple PPR Protein Interactions Are Involved in the RNA Editing System in Arabidopsis Mitochondria and Plastids.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 114 (33): 8883–88. https://doi.org/10.1073/pnas.1705815114.
Chicago author-date (all authors)
Andres Colas, Nuria, Qiang Zhu, Mizuki Takenaka, Bert De Rybel, Dolf Weijers, and Dominique Van Der Straeten. 2017. “Multiple PPR Protein Interactions Are Involved in the RNA Editing System in Arabidopsis Mitochondria and Plastids.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 114 (33): 8883–8888. doi:10.1073/pnas.1705815114.
Vancouver
1.
Andres Colas N, Zhu Q, Takenaka M, De Rybel B, Weijers D, Van Der Straeten D. Multiple PPR protein interactions are involved in the RNA editing system in Arabidopsis mitochondria and plastids. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2017;114(33):8883–8.
IEEE
[1]
N. Andres Colas, Q. Zhu, M. Takenaka, B. De Rybel, D. Weijers, and D. Van Der Straeten, “Multiple PPR protein interactions are involved in the RNA editing system in Arabidopsis mitochondria and plastids,” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 114, no. 33, pp. 8883–8888, 2017.
@article{8531126,
  abstract     = {{Recent identification of several different types of RNA editing factors in plant organelles suggests complex RNA editosomes within which each factor has a different task. However, the precise protein interactions between the different editing factors are still poorly understood. In this paper, we show that the E+-type pentatricopeptide repeat (PPR) protein SLO2, which lacks a C-terminal cytidine deaminase-like DYW domain, interacts in vivo with the DYW-type PPR protein DYW2 and the P-type PPR protein NUWA in mitochondria, and that the latter enhances the interaction of the former ones. These results may reflect a protein scaffold or complex stabilization role of NUWA between E+-type PPR and DYW2 proteins. Interestingly, DYW2 and NUWA also interact in chloroplasts, and DYW2-GFP overexpressing lines show broad editing defects in both organelles, with predominant specificity for sites edited by E+-type PPR proteins. The latter suggests a coordinated regulation of organellar multiple site editing through DYW2, which probably provides the deaminase activity to E+ editosomes.}},
  author       = {{Andres Colas, Nuria and Zhu, Qiang and Takenaka, Mizuki and De Rybel, Bert and Weijers, Dolf and Van Der Straeten, Dominique}},
  issn         = {{0027-8424}},
  journal      = {{PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA}},
  keywords     = {{DYW2,NUWA,PPR,RNA editing,SLO2,PENTATRICOPEPTIDE REPEAT PROTEINS,SUBCELLULAR-LOCALIZATION,PLANT-MITOCHONDRIA,DYW DOMAIN,IDENTIFICATION,RECOGNITION,SITE,PEROXISOMES,MACHINERY,THALIANA}},
  language     = {{eng}},
  number       = {{33}},
  pages        = {{8883--8888}},
  title        = {{Multiple PPR protein interactions are involved in the RNA editing system in Arabidopsis mitochondria and plastids}},
  url          = {{http://doi.org/10.1073/pnas.1705815114}},
  volume       = {{114}},
  year         = {{2017}},
}

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