A hypothesis on the identification of the editing enzyme in plant organelles

FEBS Lett. 2007 Sep 4;581(22):4132-8. doi: 10.1016/j.febslet.2007.07.075. Epub 2007 Aug 10.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cytidine Deaminase / chemistry
  • Cytidine Deaminase / metabolism
  • Databases, Protein
  • Models, Biological*
  • Molecular Sequence Data
  • Organelles / enzymology*
  • Organelles / genetics*
  • Phylogeny
  • Plants / enzymology*
  • Plants / genetics*
  • Protein Structure, Tertiary
  • RNA Editing / genetics*

Substances

  • Cytidine Deaminase