Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 24, Pages 21361-21371Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.230516
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Funding
- Australian Research Council [CE0561495]
- Australian Government Department of Innovation, Industry, Science and Research [CG120098]
- Centre National de la Recherche Scientifique
- Deutsche Forschungsgeminschaft
- Region of Alsace
- University of Western Australia
- Ministry of Education, Culture, Sport, Science, and Technology of Japan [17GS0316, 16085206]
- Genomics for Agricultural Innovation, Ministry of Agriculture, Forestry, and Fishers of Japan [GPN0008]
- Grants-in-Aid for Scientific Research [17GS0316, 22870029, 16085206, 23657032] Funding Source: KAKEN
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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.
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