Published online 7 December 2004
Nucleic Acids Research, Vol. 32 No. 21 © Oxford University Press 2004; all rights reserved
Different patterns in the recognition of editing sites in plant mitochondria
Laboratoire de Réplication et Expression des Génomes Eucaryotes et Rétroviraux, UMR 5097, Centre National de la Recherche Scientifique and Université Victor Segalen-Bordeaux II 146, rue Leo Saignat 33076 Bordeaux Cedex, France and 1 Departamento de Genética Molecular y Microbiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Casilla 114-D, Santiago, Chile
* To whom correspondence should be addressed. Tel: +33 5 57 57 17 46; Fax: +33 5 57 57 17 66; Email: Alexandre.Araya{at}reger.u-bordeaux2.fr
Present address: Jean-Claude Farré, Section of Molecular Biology, University of California, San Diego, La Jolla, CA 92093, USA
Received September 30, 2004; Revised and Accepted November 10, 2004
Higher plant mitochondrial mRNAs are extensively modified by highly specific C-to-U conversions. However, the determinants of recognition specificity are, to date, unknown. Here, we analyse the cis-elements involved in the recognition of two editing sites in a cox2 gene in wheat mitochondria. A minimal region of 23 nt was found to be involved in recognition of the editing site C77, similar to our previous report for site C259. These regions were correctly recognized by the mitochondrial editing machinery when placed elsewhere in the transcript. The nearest neighbour residues of the target C play a crucial role in editing, but the nature and position of the residue varies according to the editing site concerned. The target region seems to be formed by two regions 5' and 3', which can be separated by a maximum of two residues. Studies on single residue mutants concerning every position in the 23 nt region indicated that editing sites are affected differently by their neighbouring sequences. These results suggest that, notwithstanding the similar extent and location of cis-elements, the editing site recognition mechanisms may differ in plant mitochondria.
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