Involvement of DNA ligase III and ribonuclease H1 in mitochondrial DNA replication in cultured human cells
Open accessAbstract
Recent evidence suggests that coupled leading and lagging strand DNA synthesis operates in mammalian mitochondrial DNA (mtDNA) replication, but the factors involved in lagging strand synthesis are largely uncharacterised. We investigated the effect of knockdown of the candidate proteins in cultured human cells under conditions where mtDNA appears to replicate chiefly via coupled leading and lagging strand DNA synthesis to restore the copy number of mtDNA to normal levels after transient mtDNA depletion. DNA ligase III knockdown attenuated the recovery of mtDNA copy number and appeared to cause single strand nicks in replicating mtDNA molecules, suggesting the involvement of DNA ligase III in Okazaki fragment ligation in human mitochondria. Knockdown of ribonuclease (RNase) H1 completely prevented the mtDNA copy number restoration, and replication intermediates with increased single strand nicks were readily observed. On the other hand, knockdown of neither flap endonuclease 1 (FEN1) nor DNA2 affected mtDNA replication. These findings imply that RNase H1 is indispensable for the progression of mtDNA synthesis through removing RNA primers from Okazaki fragments. In the nucleus, Okazaki fragments are ligated by DNA ligase I, and the RNase H2 is involved in Okazaki fragment processing. This study thus proposes that the mitochondrial replication system utilises distinct proteins, DNA ligase III and RNase H1, for Okazaki fragment maturation.
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Knockdown of RNase H1 in human bone osteosarcoma cells (143B TK-) led to lower mtDNA copy number and complete stalling of replication.
“Knockdown of RNase H1 in human bone osteosarcoma cells (143B TK-) led to lower mtDNA copy number and complete stalling of replication (Ruhanen et al., 2011), suggesting RNase H1 is vital for mtDNA replication.”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Ruhanen et al., 2011
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- Authors
- Ruhanen, H., Ushakov, K., & Yasukawa, T.
- Affiliations
- University College London (GB)
- Corresponding author
- Yasukawa, Takehiro
- ORCID
- Yasukawa, Takehiro
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2011-12
- Volume
- 1813
- Issue
- 12
- Pages
- 2000-2007
- ISSN
- 0167-4889 (ISSN-L)
- PMC
- PMC3223524
- OpenAlex
- W2089855332
- Cited by
- 41
- References
- 35
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2022: 1 · 2021: 8 · 2020: 3 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 4 · 2015: 4 · 2014: 4 · 2013: 1 · 2012: 2
- FWCI
- 0.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council David Phillips Fellowship
- University of London Central Research Fund
- CRDC Funding from UCLH Charities and UCL Medical School
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- mitochondrial DNA replication, DNA ligase III, RNase H1, lagging strand synthesis, mitochondrial DNA copy number, RNA primer removal, FEN1, DNA2, single-strand nicks, mtDNA depletion, human cells
- MeSH terms
- DNA Ligase ATP, Poly-ADP-Ribose Binding Proteins, Bone Neoplasms, DNA, DNA Replication, DNA, Mitochondrial, Humans, DNA Ligases, Osteosarcoma, Thymidine Kinase, Tumor Cells, Cultured, Blotting, Southern, Blotting, Western, Ribonuclease H, Xenopus Proteins, Flap Endonucleases
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