The Analysis of the Editing Defects in the <i>dyw2</i> Mutant Provides New Clues for the Prediction of RNA Targets of Arabidopsis E+-Class PPR Proteins
Bastien Malbert,
Matthias Burger,
Mauricio Lopez-Obando,
Kevin Baudry,
Alexandra Launay-Avon,
Barbara Härtel,
Daniil Verbitskiy,
Anja Jörg,
Richard Berthomé,
Claire Lurin,
Mizuki Takenaka,
Etienne Delannoy
Affiliations
Bastien Malbert
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
Matthias Burger
Molekulare Botanik, Universität Ulm, 89069 Ulm, Germany
Mauricio Lopez-Obando
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
Kevin Baudry
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
Alexandra Launay-Avon
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
Barbara Härtel
Molekulare Botanik, Universität Ulm, 89069 Ulm, Germany
Daniil Verbitskiy
Molekulare Botanik, Universität Ulm, 89069 Ulm, Germany
Anja Jörg
Molekulare Botanik, Universität Ulm, 89069 Ulm, Germany
Richard Berthomé
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
Claire Lurin
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
Mizuki Takenaka
Molekulare Botanik, Universität Ulm, 89069 Ulm, Germany
Etienne Delannoy
Institute of Plant Sciences Paris-Saclay (IPS2), Université Paris-Saclay, CNRS, INRAE, Univ Evry, 91405 Orsay, France
C to U editing is one of the post-transcriptional steps which are required for the proper expression of chloroplast and mitochondrial genes in plants. It depends on several proteins acting together which include the PLS-class pentatricopeptide repeat proteins (PPR). DYW2 was recently shown to be required for the editing of many sites in both organelles. In particular almost all the sites associated with the E+ subfamily of PPR proteins are depending on DYW2, suggesting that DYW2 is required for the function of E+-type PPR proteins. Here we strengthened this link by identifying 16 major editing sites controlled by 3 PPR proteins: OTP90, a DYW-type PPR and PGN and MEF37, 2 E+-type PPR proteins. A re-analysis of the DYW2 editotype showed that the 49 sites known to be associated with the 18 characterized E+-type PPR proteins all depend on DYW2. Considering only the 288 DYW2-dependent editing sites as potential E+-type PPR sites, instead of the 795 known editing sites, improves the performances of binding predictions systems based on the PPR code for E+-type PPR proteins. However, it does not compensate for poor binding predictions.