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The cytidine deaminase signature H x E (x) n C xx C of DYW 1 binds zinc and is necessary for RNA editing of ndh D ‐1
Author(s) -
Boussardon Clément,
Avon Alexandra,
Kindgren Peter,
Bond Charles S.,
Challenor Michael,
Lurin Claire,
Small Ian
Publication year - 2014
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.12928
Subject(s) - rna editing , cytidine , cytidine deaminase , pentatricopeptide repeat , rna , biology , biochemistry , rna binding protein , amino acid , enzyme , gene
Summary 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 DYW 1, an editing factor required for editing of the ndh D ‐1 site in A rabidopsis 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 DYW 1 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.