Mitochondria are the main source of ATP production and also contribute to many other processes central to cellular function. Mitochondrial activities have been linked with growth, differentiation and aging. As relicts of bacterial endosymbionts, these organelles contain their own genetic system (i.e., mitogenome or mtDNA). The expression of the mtDNA in plants is complex, particularly at the posttranscriptional level. Following transcription, the polycistronic pre-RNAs in plant mitochondria are processed into individual RNAs, which then undergo extensive modifications, as trimming, splicing and C→U editing, before being translated by organellar ribosomes. Our study focuses on N 6 -methylation of Adenosine ribonucleotides (m 6 A-RNA) in plant mitochondria. m 6 A is the most common modification in eukaryotic mRNAs. The biological significance of this highly dynamic modification is under investigation, but it's widely accepted that m 6 A mediates structural switches that affect RNA stability and activity. By performing m 6 A-pulldown/RNA-seq (m 6 A-RIP-seq) analyses of Arabidopsis and cauliflower mitochondrial transcripts (mtRNAs), we provide with detail information on the m 6 A landscapes in angiosperms mitochondria. The results indicate that m 6 A targets different types of mtRNAs, including coding sequences, UTRs, introns and non-coding RNA species. While introns and noncoding-RNAs undergo multiple m 6 A modifications along the transcript, in mRNAs m 6 A-modifications are preferably positioned near start-codons, and may modulate the translatability of the m 6 A-modified transcripts. The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase. FEBS Lett, 540, 201-205. . (2010) Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities. A. and Erlacher, M.D. (2016) Nucleotide modifications within bacterial messenger RNAs regulate their translation and are able to rewire the genetic code. Nucleic Acids Res, 44, 852-862.