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

Nuria Andrés-Colás, Qiang Zhu, Mizuki Takenaka, Bert De Rybel, Dolf Weijers, Dominique Van Der Straeten*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

43 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)8883-8888
JournalProceedings of the National Academy of Sciences of the United States of America
Volume114
Issue number33
DOIs
Publication statusPublished - 2017

Keywords

  • DYW2
  • NUWA
  • PPR
  • RNA editing
  • SLO2

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