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A hypothesis on the identification of the editing enzyme in plant organelles
Author(s) -
Salone Véronique,
Rüdinger Mareike,
Polsakiewicz Monika,
Hoffmann Beate,
Groth-Malonek Milena,
Szurek Boris,
Small Ian,
Knoop Volker,
Lurin Claire
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.075
Subject(s) - pentatricopeptide repeat , rna editing , cytidine , organelle , biology , rna , enzyme , biochemistry , computational biology , gene
RNA editing in plant organelles is an enigmatic process leading to conversion of cytidines into uridines. Editing specificity is determined by proteins; both those known so far are pentatricopeptide repeat (PPR) proteins. The enzyme catalysing RNA editing in plants is still totally unknown. We propose that the DYW domain found in many higher plant PPR proteins is the missing catalytic domain. This hypothesis is based on two compelling observations: (i) the DYW domain contains invariant residues that match the active site of cytidine deaminases; (ii) the phylogenetic distribution of the DYW domain is strictly correlated with RNA editing.