Editing status of mat-r transcripts in mitochondria from two plant species: C-to-U changes occur in putative functional RT and maturase domains

Begu, D; Farre J.-C.; Araya, A; Mercado, A.; Holuigue, L; Jordana, X; Moenne, A

Keywords: sequence, acid, proteins, isolation, dna, transcription, binding, protein, plant, gene, mitochondria, polymerase, sites, potato, wheat, rna, homology, drug, molecular, data, article, mitochondrial, base, cytosine, genetic, uracil, codon, controlled, intron, reading, vegetable, frame, study, nucleotide, solanum, amino, priority, nonhuman, journal, Homology,, DNA,, Transcription,, open, Genes,, editing, Triticum, aestivum, unclassified, tuberosum, directed, Analysis,, cytidine, uridine, RNA-Directed, Nucleotidyltransferases, maturase, Endoribonucleases

Abstract

The intronic mat-r ORF encodes a protein with significant homology to retroviral reverse transcriptases. Here, we describe the nucleotide sequence of potato mat-r and study the editing status of mat-r transcripts in two systems, potato and wheat, where the mat-r ORF is part of the trans-introns but in two different configurations relative to nad1 exons d and e. In potato and wheat, 13 and 15 C-to-U transitions respectively were observed. Most transcripts were partially edited, but potato transcripts were edited more efficiently than wheat transcripts. As in functional mitochondrial genes, RNA editing increased the similarity between plant mat-r proteins and their homologous non-plant counterparts. Interestingly, editing of mat-r was clustered in the reverse-transcriptase (RT) and the maturase (X) domains, two well defined regions having known functions in other systems. These results, together with the integrity and sequence conservation of mat-r, strongly suggest that the encoded protein plays a functional role in plant mitochondria.

Más información

Título de la Revista: CURRENT GENETICS
Volumen: 33
Número: 6
Editorial: Springer
Fecha de publicación: 1998
Página de inicio: 420
Página final: 428
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-0031848740&partnerID=q2rCbXpz