A hypothesis on the identification of the editing enzyme in plant organelles
Autor: | Mareike Rüdinger, Ian Small, Beate Hoffmann, Claire Lurin, Véronique Salone, Boris Szurek, Monika Polsakiewicz, Volker Knoop, Milena Groth-Malonek |
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Jazyk: | angličtina |
Předmět: |
RNA editing
DYW domain Molecular Sequence Data Biophysics PPR protein Models Biological Biochemistry chemistry.chemical_compound Plant evolution Protein structure Structural Biology Phylogenetics Cytidine Deaminase Genetics Amino Acid Sequence Binding site Databases Protein Molecular Biology Peptide sequence Phylogeny Organelles Binding Sites biology Active site Cytidine Cell Biology Plants Protein Structure Tertiary chemistry biology.protein Pentatricopeptide repeat |
Zdroj: | FEBS Letters. (22):4132-4138 |
ISSN: | 0014-5793 |
DOI: | 10.1016/j.febslet.2007.07.075 |
Popis: | 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. |
Databáze: | OpenAIRE |
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