One C-to-U RNA Editing Site and Two Independently Evolved Editing Factors: Testing Reciprocal Complementation with DYW-Type PPR Proteins from the Moss Physcomitrium (Physcomitrella) patens and the Flowering Plants Macadamia integrifolia and Arabidopsis

DYW-type PPR proteins independently evolved in mosses and flowering plants restore RNA editing defects across wide phylogenetic distances. Abstract Cytidine-to-uridine RNA editing is a posttranscriptional process in plant organelles, mediated by specific pentatricopeptide repeat (PPR) proteins. In a...

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Bibliographic Details
Published in:The Plant cell 2020-09, Vol.32 (9), p.2997-3018
Main Authors: Oldenkott, Bastian, Burger, Matthias, Hein, Anke-Christiane, Jörg, Anja, Senkler, Jennifer, Braun, Hans-Peter, Knoop, Volker, Takenaka, Mizuki, Schallenberg-Rüdinger, Mareike
Format: Article
Language:English
Subjects:
Arabidopsis - genetics
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
Bryopsida - genetics
Evolution, Molecular
Gene Knockout Techniques
Genetic Complementation Test
Macadamia - genetics
Mitochondria - genetics
Mitochondria - metabolism
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phylogeny
Plants, Genetically Modified
RNA Editing
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
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Summary:DYW-type PPR proteins independently evolved in mosses and flowering plants restore RNA editing defects across wide phylogenetic distances. Abstract Cytidine-to-uridine RNA editing is a posttranscriptional process in plant organelles, mediated by specific pentatricopeptide repeat (PPR) proteins. In angiosperms, hundreds of sites undergo RNA editing. By contrast, only 13 sites are edited in the moss Physcomitrium (Physcomitrella) patens. Some are conserved between the two species, like the mitochondrial editing site nad5eU598RC. The PPR proteins assigned to this editing site are known in both species: the DYW-type PPR protein PPR79 in P. patens and the E+-type PPR protein CWM1 in Arabidopsis (Arabidopsis thaliana). CWM1 also edits sites ccmCeU463RC, ccmBeU428SL, and nad5eU609VV. Here, we reciprocally expressed the P. patens and Arabidopsis editing factors in the respective other genetic environment. Surprisingly, the P. patens editing factor edited all target sites when expressed in the Arabidopsis cwm1 mutant background, even when carboxy-terminally truncated. Conversely, neither Arabidopsis CWM1 nor CWM1-PPR79 chimeras restored editing in P. patens ppr79 knockout plants. A CWM1-like PPR protein from the early diverging angiosperm macadamia (Macadamia integrifolia) features a complete DYW domain and fully rescued editing of nad5eU598RC when expressed in P. patens. We conclude that (1) the independently evolved P. patens editing factor PPR79 faithfully operates in the more complex Arabidopsis editing system, (2) truncated PPR79 recruits catalytic DYW domains in trans when expressed in Arabidopsis, and (3) the macadamia CWM1-like protein retains the capacity to work in the less complex P. patens editing environment.
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.20.00311