Acta Scientific Pharmaceutical Sciences (ASPS)(ISSN: 2581-5423)

Review Article Volume 5 Issue 12

RNA Processing and Degradation in Eukaryotic Cells’ Mitochondria

Vahideh Hamidi Sofiani1, Arefeh Ebrahimian Shiadeh1, Mohammadreza Kalani2 and Abdolvahab Moradi1*

1Department of Microbiology, Golestan University of Medical Sciences, Gorgan, Iran
2Department of Molecular Medicine, Golestan University of Medical Sciences, Golestan, Iran

*Corresponding Author: Abdolvahab Moradi, Department of Microbiology, Golestan University of Medical Sciences, Gorgan, Iran.

Received: September 12, 2021; Published: November 16, 2021


The mammalian mitochondrial genome can encode tRNAs, rRNAs, and mRNA. Moreover, the mitochondrion is an important site for RNA degradation phenomenon in addition to transcriptional duties, however, there are different assumptions related to this phenomenon. It has been suggested that the presence of RNA granules along with a variety of enzymes in the mitochondria may be involved in the RNA degradation process. In this paper, we try to investigate the factors affecting RNA degradation in mitochondria.

Keywords: Mitochondria; RNA; mRNA


  1. Barchiesi A and Vascotto C. “Transcription, processing, and decay of mitochondrial RNA in health and disease”. International Journal of Molecular Sciences 9 (2019): 2221.
  2. De Vries R. “DNA condensation in bacteria: Interplay between macromolecular crowding and nucleoid proteins”. Biochimie12 (2010): 1715-1721.
  3. Kvist L., et al. “Paternal leakage of mitochondrial DNA in the great tit (Parus major)”. Molecular Biology and Evolution 2 (2003): 243-247.
  4. Iborra FJ., et al. “The functional organization of mitochondrial genomes in human cells”. BMC Biology1 (2004): 1-14.
  5. Masters BS., et al. “Yeast mitochondrial RNA polymerase is homologous to those encoded by bacteriophages T3 and T7”. Cell1 (1987): 89-99.
  6. Cotney J., et al. “Relative abundance of the human mitochondrial transcription system and distinct roles for h-mtTFB1 and h-mtTFB2 in mitochondrial biogenesis and gene expression”. Nucleic Acids Research12 (2007): 4042-4054.
  7. Falkenberg M., et al. “Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA”. Nature Genetics3 (2002): 289-294.
  8. Minczuk M., et al. “TEFM (c17orf42) is necessary for transcription of human mtDNA”. Nucleic Acids Research10 (2011): 4284-4299.
  9. Shi Y., et al. “Mammalian transcription factor A is a core component of the mitochondrial transcription machinery”. Proceedings of the National Academy of Sciences41 (2012): 16510-16515.
  10. Agaronyan K., et al. “Replication-transcription switch in human mitochondria”. Science6221 (2015): 548-551.
  11. Posse V., et al. “TEFM is a potent stimulator of mitochondrial transcription elongation in vitro”. Nucleic Acids Research5 (2015): 2615-2624.
  12. Mai N., et al. “The process of mammalian mitochondrial protein synthesis”. Cell and Tissue Research 1 (2017): 5-20.
  13. Pearce SF., et al. “Regulation of mammalian mitochondrial gene expression: recent advances”. Trends in Biochemical Sciences 8 (2017): 625-639.
  14. Borowski LS., et al. “Human mitochondrial RNA decay mediated by PNPase–hSuv3 complex takes place in distinct foci”. Nucleic Acids Research 2 (2013): 1223-1240.
  15. Barrientos A. “Mitochondriolus: assembling Mito ribosomes”. Oncotarget19 (2015): 16800.
  16. Tu Y-T and Barrientos A. “The human mitochondrial DEAD-box protein DDX28 resides in RNA granules and functions in Mito ribosome assembly”. Cell Reports6 (2015): 854-864.
  17. Anderson S., et al. “Sequence and organization of the human mitochondrial genome”. Nature5806 (1981): 457-465.
  18. Ojala D., et al. “tRNA punctuation model of RNA processing in human mitochondria”. Nature5806 (1981): 470-474.
  19. Antonicka H., et al. “The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression”. Cell Metabolism3 (2013): 386-398.
  20. Jourdain AA., et al. “GRSF1 regulates RNA processing in mitochondrial RNA granules”. Cell Metabolism3 (20133): 399-410.
  21. Lee K-W., et al. “Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid”. Journal of Biological Chemistry43 (2013): 31386-31399.
  22. Holzmann J., et al. “RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme”. Cell 3 (2008): 462-474.
  23. Sokhi UK., et al. “Human Polynucleotide Phosphorylase (hPNPaseold-35): Should I Eat You or Not—That Is the Question?” In: Tew KD, Fisher PB, editors. Advances in Cancer Research 119 (2013) 161-190.
  24. Bruni F., et al. “REXO2 is an oligoribonuclease active in human mitochondria”. Plos One5 (2013): e64670.
  25. Cameron TA., et al. “Polynucleotide phosphorylase: Not merely an RNase but a pivotal post-transcriptional regulator”. Plos Genetics10 (2018): e1007654.
  26. Wang DD-H., et al. “Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3′-to-5′ directionality”. Journal of Biological Chemistry31 (2009): 20812-20821.
  27. Chen H-W., et al. “Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis”. Molecular and Cellular Biology 2006;26.22 (2006): 8475-8487.
  28. Pietras Z., et al. “Controlling the mitochondrial antisense–role of the SUV3-PNPase complex and its co-factor GRSF1 in mitochondrial RNA surveillance”. Molecular and Cellular Oncology6 (2018): e1516452.
  29. Antonicka H., et al. “The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression”. Cell Metabolism3 (2013): 386-398.
  30. Sterky FH., et al. “LRPPRC is a mitochondrial matrix protein that is conserved in metazoans”. Biochemical and Biophysical Research Communications4 (2010): 759-764.
  31. Baughman JM., et al. “Correction: A Computational Screen for Regulators of Oxidative Phosphorylation Implicates SLIRP in Mitochondrial RNA Homeostasis”. Plos Genetics3 (2010).
  32. Levy S., et al. “Identification of LACTB2, a metallo-β-lactamase protein, as a human mitochondrial”. Nucleic Acids Research4 (2016): 1813-1832.
  33. Holzmann J., et al. “RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme”. Cell 3 (2008): 462-474.


Citation: Abdolvahab Moradi., et al. “RNA Processing and Degradation in Eukaryotic Cells’ Mitochondria". Acta Scientific Pharmaceutical Sciences 5.12 (2021): 58-62.


Copyright: © 2021 Abdolvahab Moradi., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


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