FEBS Letters
Volume 581, Issue 22 , Pages 4132-4138, 4 September 2007

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

Edited by Micheal R. Sussman

  • Véronique Salone

      Affiliations

    • URGV, 2 Rue Gaston Crémieux, F-91057 Evry Cedex, France
    • ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009, Australia
  • ,
  • Mareike Rüdinger

      Affiliations

    • IZMB, Abt. Molekulare Evolution, Kirschallee 1, D-53115 Bonn, Germany
  • ,
  • Monika Polsakiewicz

      Affiliations

    • IZMB, Abt. Molekulare Evolution, Kirschallee 1, D-53115 Bonn, Germany
  • ,
  • Beate Hoffmann

      Affiliations

    • URGV, 2 Rue Gaston Crémieux, F-91057 Evry Cedex, France
  • ,
  • Milena Groth-Malonek

      Affiliations

    • IZMB, Abt. Molekulare Evolution, Kirschallee 1, D-53115 Bonn, Germany
  • ,
  • Boris Szurek

      Affiliations

    • URGV, 2 Rue Gaston Crémieux, F-91057 Evry Cedex, France
  • ,
  • Ian Small

      Affiliations

    • URGV, 2 Rue Gaston Crémieux, F-91057 Evry Cedex, France
    • ARC Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009, Australia
  • ,
  • Volker Knoop

      Affiliations

    • IZMB, Abt. Molekulare Evolution, Kirschallee 1, D-53115 Bonn, Germany
  • ,
  • Claire Lurin

      Affiliations

    • URGV, 2 Rue Gaston Crémieux, F-91057 Evry Cedex, France
    • Corresponding Author InformationCorresponding author. Fax: +33 1 60 87 45 10.

Received 31 May 2007; received in revised form 20 July 2007; accepted 30 July 2007. published online 13 August 2007.

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.

Keywords: RNA editing, PPR protein, DYW domain, Plant evolution

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PII: S0014-5793(07)00856-3

doi:10.1016/j.febslet.2007.07.075

FEBS Letters
Volume 581, Issue 22 , Pages 4132-4138, 4 September 2007