title: The pentatricopeptide repeat protein OTP87 is essential for RNA editing of nad7 and atp1 transcripts in Arabidopsis mitochondria.
abstract: In plant organelles, RNA editing is a post-transcriptional mechanism that converts specific cytidines to uridines in RNA of both mitochondria and plastids, altering the information encoded by the gene. The cytidine to be edited is determined by a cis-element surrounding the editing site that is specifically recognized and bound by a trans-acting factor. All the trans-acting editing factors identified so far in plant organelles are members of a large protein family, the pentatricopeptide repeat (PPR) proteins. We have identified the Organelle Transcript Processing 87 (OTP87) gene, which is required for RNA editing of the nad7-C24 and atp1-C1178 sites in Arabidopsis mitochondria. OTP87 encodes an E-subclass PPR protein with an unusually short E-domain. The recombinant protein expressed in Escherichia coli specifically binds to RNAs comprising 30 nucleotides upstream and 10 nucleotides downstream of the nad7-C24 and atp1-C1178 editing sites. The loss-of-function of OTP87 results in small plants with growth and developmental delays. In the otp87 mutant, the amount of assembled respiratory complex V (ATP synthase) is highly reduced compared with the wild type suggesting that the amino acid alteration in ATP1 caused by loss of editing at the atp1-C1178 site affects complex V assembly in mitochondria.
authors.affiliation: Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley 6009 Western Australia, Australia. khammani@uoregon.edu
authors.forename: Kamel
authors.initials: K
authors.lastname: Hammani
authors.forename: Catherine Colas
authors.initials: CC
authors.lastname: des Francs-Small
authors.forename: Mizuki
authors.initials: M
authors.lastname: Takenaka
authors.forename: Sandra K
authors.initials: SK
authors.lastname: Tanz
authors.forename: Kenji
authors.initials: K
authors.lastname: Okuda
authors.forename: Toshiharu
authors.initials: T
authors.lastname: Shikanai
authors.forename: Axel
authors.initials: A
authors.lastname: Brennicke
authors.forename: Ian
authors.initials: I
authors.lastname: Small
mesh_terms: D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000502:physiology*; D001665:Binding Sites; D002734:Chlorophyll / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D005816:Genetic Complementation Test; D008928:Mitochondria / Q000378:metabolism*; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism; D008957:Models, Genetic; D009154:Mutation; D009245:NADH Dehydrogenase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010641:Phenotype; D010940:Plant Proteins / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D017393:RNA Editing; D016601:RNA-Binding Proteins / Q000502:physiology*
chemical_list: C560634:ATP1 protein, Arabidopsis; D029681:Arabidopsis Proteins; C560632:OTP87 protein, Arabidopsis; D010455:Peptides; D010940:Plant Proteins; D016601:RNA-Binding Proteins; D002734:Chlorophyll; C560633:NAD7 protein, Arabidopsis; D009245:NADH Dehydrogenase; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases