Journal
NEW PHYTOLOGIST
Volume 203, Issue 4, Pages 1090-1095Publisher
WILEY-BLACKWELL
DOI: 10.1111/nph.12928
Keywords
cytidine deaminase; DYW domain; pentatricopeptide repeat (PPR) proteins; RNA editing; zinc-binding motif
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Funding
- Australian Research Council Centre of Excellence grants [CE0561495, CE140100008]
- Australian Government International Science Linkages grants [FR060030, CG120098]
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In flowering plants, RNA editing involves deamination of specific cytidines to uridines in both mitochondrial and chloroplast transcripts. Pentatricopeptide repeat (PPR) proteins and multiple organellar RNA editing factor (MORF) proteins have been shown to be involved in RNA editing but none have been shown to possess cytidine deaminase activity. The DYW domain of some PPR proteins contains a highly conserved signature resembling the zinc-binding active site motif of known nucleotide deaminases. We modified these highly conserved amino acids in the DYW motif of DYW1, an editing factor required for editing of the ndhD-1 site in Arabidopsis chloroplasts. We demonstrate that several amino acids of this signature motif are required for RNA editing in vivo and for zinc binding in vitro. We conclude that the DYW domain of DYW1 has features in common with cytidine deaminases, reinforcing the hypothesis that this domain forms part of the active enzyme that carries out RNA editing in plants.
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