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PMID: 17707818 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 581 ·No. 22 ·2007-09-04 ·Pages 4132-8

Salone V, Rüdinger M, Polsakiewicz M, Hoffmann B, Groth-Malonek M, Szurek B, Small I, Knoop V, Lurin C

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.

MeSH Terms
Amino Acid Sequence Binding Sites Cytidine Deaminase/chemistry,metabolism Databases, Protein Models, Biological Molecular Sequence Data Organelles/enzymology,genetics Phylogeny Plants/enzymology,genetics Protein Structure, Tertiary RNA Editing/genetics
Chemicals
Cytidine Deaminase
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Salone Véronique
URGV, 2 Rue Gaston Crémieux, F-91057 Evry Cedex, France.
Rüdinger Mareike
Polsakiewicz Monika
Hoffmann Beate
Groth-Malonek Milena
Szurek Boris
Small Ian
Knoop Volker
Lurin Claire
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2007-09-04
Epub
2007-00-10
Pages
4132-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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