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Template Properties of 5-Methyl-2'-Deoxycytidine and 5-Hydroxymethyl-2'-Deoxycytidine in Reactions with Human Translesion and Reparative DNA Polymerases

Authors
  • Shilkin, E. S.1
  • Petrova, D. V.2
  • Poltorachenko, V. A.1
  • Boldinova, E. O.1
  • Zharkov, D. O.2, 3
  • Makarova, A. V.1
  • 1 Institute of Molecular Genetics, Kurchatov Institute Research Center, Moscow, 123182, Russia , Moscow (Russia)
  • 2 Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russia , Novosibirsk (Russia)
  • 3 Novosibirsk State University, Novosibirsk, 630090, Russia , Novosibirsk (Russia)
Type
Published Article
Journal
Molecular Biology
Publisher
Pleiades Publishing
Publication Date
Mar 01, 2021
Volume
55
Issue
2
Pages
267–272
Identifiers
DOI: 10.1134/S0026893321020138
Source
Springer Nature
Keywords
License
Yellow

Abstract

Abstract—5-Methyl-2'-deoxycytidine (mC) and the product of its controlled oxidation, 5-hydroxymethyl-2'-cytidine (hmC), play a key role in the epigenetic regulation of gene expression, the cell differentiation, and the carcinogenesis. Due to spontaneious deamination, genomic CpG sites containing mC and hmC serve as mutagenesis hotspots. In addition, error-prone translesion and reparative DNA polymerases may serve as additional source of mutations in the lesion-containing regions with CpG sites. In the present work, we performed in vitro analysis of the accuracy of nucleotide incorporation opposite to mC and hmC by human DNA polymerases Polβ, Polλ, Polη, Polι, Polκ and primase polymerase PrimPol. The results of the study show a high accuracy of copying mC and hmC by the reparative DNA polymerases Polβ and Polλ, while Polη, Polι, Polκ, and PrimPol copied mC and hmC with less accuracy evident by incorporation of dAMP and dTMP. The same spectrum of error-prone dNMP incorporation was also noted at sites with unmodified cytosines.

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