ArticleNucleic acids research2014
Transition-state destabilization reveals how human DNA polymerase β proceeds across the chemically unstable lesion N7-methylguanine.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
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- For the Better or for the Worse? The Effect of Manganese on the Activity of Eukaryotic DNA Polymerases.International journal of molecular sciences · 2023Review
- Polymeric nanoparticles for DNA vaccine-based cancer immunotherapy: a review.Biotechnology letters · 2023Review
- Genotoxic effects of the major alkylation damage N7-methylguanine and methyl formamidopyrimidine.The Biochemical journal · 2023Article
- Effect of N7-methylation on base pairing patterns of guanine: a DFT study.Journal of molecular modeling · 2021Article
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- Construction and validation of an immunity-related prognostic signature for breast cancer.Aging · 2020Article
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- A novel molecular-clinicopathologic nomogram to improve prognosis prediction of hepatocellular carcinoma.Aging · 2020Article
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- Structural insights into the promutagenic bypass of the major cisplatin-induced DNA lesion.The Biochemical journal · 2020Article
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4 authors.
Funding
Abstract
N7-Methyl-2'-deoxyguanosine (m7dG) is the predominant lesion formed by methylating agents. A systematic investigation on the effect of m7dG on DNA replication has been difficult due to the chemical instability of m7dG. To gain insights into the m7dG effect, we employed a 2'-fluorine-mediated transition-state destabilzation strategy. Specifically, we determined kinetic parameters for dCTP insertion opposite a chemically stable m7dG analogue, 2'-fluoro-m7dG (Fm7dG), by human DNA polymerase β (polβ) and solved three X-ray structures of polβ in complex with the templating Fm7dG paired with incoming dCTP or dTTP analogues. The kinetic studies reveal that the templating Fm7dG slows polβ catalysis ∼ 300-fold, suggesting that m7dG in genomic DNA may impede replication by some DNA polymerases. The structural analysis reveals that Fm7dG forms a canonical Watson-Crick base pair with dCTP, but metal ion coordination is suboptimal for catalysis in the polβ-Fm7dG:dCTP complex, which partially explains the slow insertion of dCTP opposite Fm7dG by polβ. In addition, the polβ-Fm7dG:dTTP structure shows open protein conformations and staggered base pair conformations, indicating that N7-methylation of dG does not promote a promutagenic replication. Overall, the first systematic studies on the effect of m7dG on DNA replication reveal that polβ catalysis across m7dG is slow, yet highly accurate.
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