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Authors: Maria I.G. Lopez Sanchez, Tim R. Mercer, Stefan M.K. Davies, Anne-Marie J. Shearwood, Karoline K.A. Nygård, Tara R. Richman, John S. Mattick, Oliver Rackham and Aleksandra Filipovska

Maria I.G. Lopez Sanchez

Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

Tim R. Mercer

Institute for Molecular Bioscience; The University of Queensland; Brisbane, QLD Australia

Stefan M.K. Davies

Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

Anne-Marie J. Shearwood

Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

Karoline K.A. Nygård

Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

Tara R. Richman

Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

John S. Mattick

Institute for Molecular Bioscience; The University of Queensland; Brisbane, QLD Australia

Oliver Rackham

Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

Aleksandra Filipovska

Corresponding author: afilipov@waimr.uwa.edu.au
Western Australian Institute for Medical Research and Centre for Medical Research; The University of Western Australia; Perth, WA Australia

Abstract:
Mammalian mitochondrial DNA is transcribed as precursor polycistronic transcripts containing 13 mRNAs, 2 rRNAs, punctuated by 22 tRNAs. The mechanisms involved in the excision of mitochondrial tRNAs from these polycistronic transcripts have remained largely unknown. We have investigated the roles of ELAC2, mitochondrial RNase P proteins 1 and 3, and pentatricopeptide repeat domain protein 1 in the processing of mitochondrial polycistronic transcripts. We used a deep sequencing approach to characterize the 5' and 3' ends of processed mitochondrial transcripts and provide a detailed map of mitochondrial tRNA processing sites affected by these proteins. We show that MRPP1 and MRPP3 process the 5' ends of tRNAs and the 5' unconventional, non tRNA containing site of the CO1 transcript. By contrast, we find that ELAC2 and PTCD1 affect the 3' end processing of tRNAs. Finally, we found that MRPP1 is essential for transcript processing, RNA modification, translation and mitochondrial respiration.

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