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Article

Accurate DNA Synthesis Across 8-Oxoadenine by Human PrimPol

by
Elizaveta O. Boldinova
1,2,
Alexander A. Kruchinin
1,2,
Polina N. Kamzeeva
1,3,
Andrey V. Aralov
3,* and
Alena V. Makarova
1,2,*
1
Institute of Gene Biology, Russian Academy of Sciences, 34/5 Vavilova St., 119334 Moscow, Russia
2
National Research Center “Kurchatov Institute”, Kurchatov sq. 1, 123182 Moscow, Russia
3
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997 Moscow, Russia
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2025, 26(14), 6796; https://doi.org/10.3390/ijms26146796
Submission received: 29 May 2025 / Revised: 23 June 2025 / Accepted: 7 July 2025 / Published: 16 July 2025
(This article belongs to the Section Molecular Biology)
Browse Figures
Versions Notes

Abstract

PrimPol is a human DNA primase and DNA polymerase involved in DNA damage tolerance in both nuclei and mitochondria. PrimPol restarts stalled replication forks by synthesizing DNA primers de novo and also possesses DNA translesion activity (TLS activity). PrimPol efficiently and relatively accurately bypasses several DNA lesions including 8-oxoguanine, thymine glycol and 5-formyluracil. In this work, we showed that PrimPol possesses efficient and accurate TLS activity across 8-oxoadenine, another common DNA lesion caused by oxidative stress. The accuracy of PrimPol on DNA with 8-oxoA was significantly higher compared to DNA containing 8-oxoG. Replacement of Mg2+ ions with Mn2+ stimulated activity of PrimPol on DNA with 8-oxoA and 8-oxoG as well as undamaged A in a sequence-dependent manner by the lesion skipping (or template scrunching) mechanism. Altogether, our data support the idea that PrimPol possesses efficient TLS activity across a wide range of DNA lesions caused by oxidative stress.

1. Introduction

Human PrimPol possesses DNA primase and DNA polymerase activities and is present in both the nucleus and mitochondria [1,2,3]. It is involved in DNA damage tolerance by the restarting of replication forks at the sites of DNA damage and non-B DNA structures such as G-quadruplexes [4,5,6,7,8,9]. Cells deficient in PrimPol are sensitive to DNA-damaging agents [3,10,11].
PrimPol also demonstrates DNA translesion activity (TLS activity) and can bypass a variety of small DNA lesions [1,12]. PrimPol is blocked on DNA with bulky N2-dG adducts [13] and DNA–protein and AP site–peptide cross-links [14,15], but can bypass and incorporate complementary nucleotides opposite the cisplatin GG cross-link [15].
Previously, we and others demonstrated that PrimPol carries out efficient and relatively accurate synthesis past DNA lesions caused by oxidation such as 8-oxoguanine (8-oxoG) and 5-formyluracil [1,12,16]. Substitution of Mg2+ with Mn2+ ions also stimulated the synthesis on DNA with thymine glycol [12]. Such efficient TLS activity might facilitate PrimPol-mediated repriming on severely damaged DNA, e.g., containing clustered DNA damage.
Along with 8-oxoG, 8-oxoadenine (8-oxoA) is the most abundant oxidative lesion [17,18,19,20] with dual miscoding properties. The number of 8-oxoA lesions ranged from 10 to 50% of 8-oxoG in [19], but was detected at the level of 0.7 lesions per 106 nucleotides, which corresponds to ~2200 lesions per human genome and is comparable with 8-oxoG levels in [20]. It was also shown that the ratio of 8-oxoA to 8-oxoG reaches 1:1 in some cancer cells [21]. These modified bases readily adopt the syn conformation: 8-oxoG forms stable 8-oxoG(syn):A(anti) Hoogsteen mispair while 8-oxoA efficiently forms the 8-oxoA(syn):G(anti) pair [22,23]. The majority of DNA polymerases preferentially incorporate non-complementary dAMP opposite 8-oxoG (the so-called “A-rule”), leading to G:C → T:A transversions [23,24]. While 8-oxoA is not mutagenic in Escherichia coli [25], its mutagenic effect was demonstrated in mammalian cells [26,27]. The 8-oxoA lesion placed in the HRAS oncogene mutation hotspot sequence stimulated A:T → C:G transversions and A:T → G:C transitions at a relatively high frequency of mutagenesis comparable [26] or 4-fold-reduced [28] in comparison to that caused by 8-oxoG.
In this work, we, for the first time, report the activity of PrimPol on DNA with 8-oxoA in the HRAS oncogene mutation hotspot sequence context. We showed that PrimPol accurately bypasses 8-oxoA in vitro. We also analyzed the effect of metal ions and DNA sequence context on the TLS activity of PrimPol on DNA with 8-oxoA and compared these data with those obtained for 8-oxoG.
Altogether, these findings further support the possible role of PrimPol in the replication of DNA with oxidative damage.

2. Results

2.1. Efficient and Accurate Bypass of 8-oxoA in Reactions in the Presence of Mg2+

First, we analyzed the activity of PrimPol in reactions in the presence of Mg2+ on DNA substrates with the HRAS oncogene sequence context 5′-CCXAG-3′ containing A, G, 8-oxoA, or 8-oxoG at the mutation hotspot in the +1 position. Both DNA lesions, 8-oxoA and 8-oxoG, only slightly inhibited the activity of PrimPol (Figure 1). Unlike many other DNA polymerases, PrimPol was more accurate and incorporated opposite 8-oxoG complementary dCMP with slight preference over non-complementary dAMP (Figure 1A,B, Table 1). However, PrimPol almost exclusively incorporated complementary dTMP opposite A and 8-oxoA (Figure 1A,B, Table 1). PrimPol incorporated non-complementary dGMP with 3- to 4-fold-reduced efficiency on the DNA template with 8-oxoA and a 10-fold reduction in efficiency on the DNA template with undamaged A compared to dTMP (Figure 1C, Table 1). Interestingly, incorporation of dGMP was observed as a ladder in reactions in the presence of DNA templates containing 8-oxoA, 8-oxoG, or undamaged A but not in reactions with template G (Figure 1A, lanes 4, 10, 16, 22). This activity can be a result of dGMP incorporation opposite C in the +2 and +3 template positions during template scrunching (or lesion skipping), leading to small deletions.

2.2. Mn2+ Ions Decrease Accuracy of PrimPol on DNA Substrates with 8-Oxopurines

The DNA polymerase activity of PrimPol as well as the template scrunching mechanism are stimulated by Mn2+ ions [12,13,29]. Indeed, replacement of Mg2+ with Mn2+ ions stimulated the activity of PrimPol and reduced its accuracy on all DNA templates (Figure 2). PrimPol carried out error-prone synthesis on DNA with 8-oxoG. Enzyme incorporated dAMP slightly more efficient than complementary dCMP (Figure 2A, lane 21, Figure 2C, Table 1).
Mn2+ ions also facilitated the incorporation of dGMP and dTMP on DNA with 8-oxoG (Figure 2A, lanes 22 and 23, Figure 2B). Mn2+ stimulated the incorporation of dGMP on both templates A and 8-oxoA (Figure 2A, lanes 4 and 16, Table 1). PrimPol was slightly more accurate on DNA with A compared to 8-oxoA in the presence of Mg2+ (Table 1). In reactions in the presence of Mn2+, PrimPol demonstrated similar accuracy by incorporating dGMP on both templates A and 8-oxoA with 4- to 7-fold-reduced efficiency (Figure 2C, Table 1). The dGMP incorporation was observed as prominent ladders on DNA with A, 8-oxoA, and 8-oxoG, and was likely a result of indels following alternative alignments with a short +2–3 CC template microhomology region.

2.3. The Effect of DNA Sequence Context on A and 8-oxoA Bypass

To test the effect of DNA sequence context on nucleotide incorporation, we replaced C in the +2 position of the HRAS oncogene sequence with A, G, or T. All replacements increased the accuracy of PrimPol and reduced the incorporation of dGMP on DNA substrates with a template containing undamaged A or 8-oxoA lesion in the presence of Mg2+ (Figure 3A,B). In reaction with Mn2+, PrimPol also incorporated dGMP on DNA templates with A and 8-oxoA in the HRAS 5′-CCXAG-3′ sequence context only (Figure 3C,D). Moreover, PrimPol incorporated dCMP on both A- and 8-oxoA-containing DNA substrates after replacement of the +2 template C with G. Altogether, these data suggest that PrimPol carries out efficient and accurate DNA synthesis across 8-oxoA. PrimPol also induces microdeletions with low efficiency in a sequence-dependent manner.

3. Discussion

8-oxoG and 8-oxoA are the most common lesions caused by reactive oxygen species. 8-oxoG is ambiguously read by DNA polymerases, leading to mutations after the next round of replication rather than showing blocking effects. The available evidence suggests that 8-oxoA in mammalian cells also has a moderate mutagenic potential and induces A:T → C:G transversions and A:T → G:C transitions in the HRAS 5′-CCXAG-3′ sequence [26,27,28].
In contrast to 8-oxoG, the activity of eukaryotic DNA polymerases opposite 8-oxoA remains poorly characterized. Only three DNA polymerases, namely Pol α, Pol β, and Pol η, have been studied to date [26,30,31]. These DNA polymerases preferentially incorporated opposite 8-oxoA dTMP and small amounts of dGMP. Pol α carried out quite accurate DNA synthesis by incorporating complementary dTMP 10-fold more efficiently compared to non-complementary dGMP [30], while translesion Pol η incorporated dTMP and dGMP with almost similar efficiency [31]. The accuracy of Pol β varied from 4- to 18-fold preference for dTMP over dGMP on DNA substrates with different sequence contexts [30,31].
Human PrimPol is a unique DNA primase involved in DNA damage tolerance pathways in both nuclei and mitochondria [1,16,32]. PrimPol can encounter DNA lesions during repriming events and also possesses DNA translesion activity. PrimPol is also known for its template scrunching activity, which can generate small deletions [29,33]. This activity is stimulated by Mn2+ and DNA lesions (lesion skipping mechanism) [12,29].
In this work, we studied PrimPol bypass of 8-oxopurine lesions in the HRAS sequence context. We demonstrated that PrimPol bypasses 8-oxoA with high efficiency and relatively high fidelity. PrimPol preferentially incorporated complementary dTMP opposite 8-oxoA in reactions in the presence of both Mg2+ and Mn2+ cofactors. PrimPol also incorporated dGMP on DNA substrates with 8-oxoA with 3- to 4-fold-reduced efficiency compared to the complementary dTMP. Unlike other DNA polymerases, dGMP incorporation by PrimPol was observed on DNA with both 8-oxoA and undamaged A. It was sequence-dependent and was stimulated by short CC nucleotide repeats in the HRAS CCXAG sequence. Replacement of C in the +2 template position abrogated dGMP incorporation, suggesting that it is mediated by the template scrunching mechanism and causes deletions.
The error-prone dGMP incorporation was observed in reactions with both Me2+ cofactors but the efficiency of dGMP incorporation was higher with Mn2+. In particular, PrimPol incorporated dGMP on DNA substrates with 8-oxoA ~3-fold less efficiently compared to undamaged A in the presence of Mg2+ ions and with equal efficiencies for both templates in reactions with Mn2+. Another type of error—dCMP incorporation on DNA templates with A or 8-oxoA—was exclusively stimulated by Mn2+ ions and was observed only in reactions with the CGXAG sequence context and guided by G in the +2 templates position. Altogether, these data are in agreement that PrimPol misincorporates nucleotides in a sequence-dependent manner utilizing the Mn2+-stimulated template scrunching mechanism, which is not specific to the 8-oxoA lesion. Our data also suggest that the rate of PrimPol-mediated errors is relatively low in all tested sequence contexts and PrimPol is unlikely to contribute to the 8-oxoA-induced mutagenesis in living cells.
The 5′-flanking nucleotide near 8-oxoG affects the accuracy of TLS by Pol η [34]. Interestingly, in our work (in the HRAS oncogene sequence context 3′-GA8-oxoGCC-5′), PrimPol demonstrated lower accuracy on DNA with 8-oxoG than in previous studies and incorporated dCMP and dAMP with almost equal efficiencies. In contrast, PrimPol incorporated dCMP almost exclusively or about 6- to 8-fold more efficiently than non-complementary dAMP in other sequence contexts such as 3′- CG8-oxoGCA-5′ [1], 3′-AG8-oxoGCA-5′ [35], 3′-TG8-oxoGAC-5′ [12], and 3′-AG8-oxoGTT-5′ [16]. Crystallographic PrimPol studies demonstrated that 8-oxoG in DNA containing the 3′-GC8-oxoGAC-5′ sequence in complex with both incoming dCTP and dATP adopts the anti or syn conformation, respectively, without significant structural hindrance within the active site, which supports the relatively low accuracy of PrimPol opposite 8-oxoG [36]. Our results corroborate these observations. It is possible that stacking interactions of 8-oxoG with flanking nucleobases contribute to its positioning in the anti or syn conformation.
Since PrimPol efficiently bypasses several DNA lesions including 8-oxoA, 8-oxoG, 5-fU, and thymine glycol, we suggest that PrimPol carries out efficient TLS across a wide range of DNA lesions caused by oxidative stress. Indeed, PrimPol attenuates the response of A549 cells to oxidative damage [37]. Also, PrimPol as a component of the MUS81-LIG4 axis takes part in replication fork restart during transcription-dependent replication stress under excessive reactive oxygen species action [38]. A recent study demonstrated that PrimPol can contribute to an SBS-A mutational signature resembling the mutagenic effect of 8-oxoG due to its ability to bypass oxidized damage [39].

4. Materials and Methods

4.1. DNA Templates and Enzymes

PrimPol was purified from E. coli as described in [15]. DNA oligonucleotides used in this study (Table 2) were synthetized as described previously [40]. 8-oxoA and 8-oxoG lesions were placed in a sequence context similar to the HRAS CCXAG mutagenesis hot spot [26] in TemplateXA. The templates TemplateXG, TemplateXT, and TemplateXC differ from TemplateXA by the single substitution at the +2 position. To prepare DNA substrates, the 5′-Cy5-labelled primer Pr18-Cy5 of 32P-labelled primer Pr18 was annealed to the corresponding unlabeled template oligonucleotides at a molar ratio of 1:1.1 in 100 mM NaCl by heating to 97 °C and slowly cooling to 4 °C.

4.2. DNA Polymerase Reactions for the Primer Extension Assay

Primer extension reactions were performed in 20 µL containing 100 nM DNA substrate, 200 μM dNTP, 30 mM HEPES pH 7.0, 10 mM MgCl2 or 1 mM MnCl2, 100 µg/mL BSA, 1 mM DTT, 4% glycerol, and 100–200 nM PrimPol. Reactions were incubated at 37 °C for 1–4 min, stopped by the addition of an equal volume of 2× loading buffer (20 mM EDTA, 0.001% bromophenol blue, 96% formamide), and heated for 5 min at 95 °C. The reaction products were resolved on 21% polyacrylamide gels with 8 M urea, visualized on Typhoon 9400 (GE Healthcare, Chicago, IL, USA), and analyzed with ImageQuant software v8.2. All experiments were repeated three times. The percent of the extended primer (PrExt) was calculated for each reaction, and the mean values of PrExt with the standard errors are shown in figures.

4.3. Steady-State Kinetics Analysis of dNMP Incorporation

To quantify the incorporation of individual dNMPs opposite DNA lesions, we varied the dNTP concentration from 2.5 to 6000 μM in reactions in the presence of 10 nM PrimPol and 10 mM MgCl2 and from 0.25 to 1000 µM in reactions with 5 nM PrimPol and 1 mM MnCl2. Depending on the lesion, the reactions were incubated for 3–20 min with MgCl2 and for 1–10 min with MnCl2 to ensure that less than 40% of the primer was utilized. Calculations were performed using GraFit 5 software (Erithacus Software, East Grinstead, UK). The data were fit to the Michaelis–Menten equation V = Vmax × [dNTP])/(KM + [dNTP]), where V and Vmax are the observed and maximum rates of the reaction (in percentages of utilized primer per minute), respectively, and KM is the apparent Michaelis constant.

Author Contributions

Methodology E.O.B., A.A.K. and P.N.K.; investigation, E.O.B., A.A.K. and P.N.K.; resources, A.V.M. and A.V.A.; data curation, E.O.B. and A.A.K.; writing—original draft preparation, A.V.M.; writing—review and editing, A.V.A.; visualization, E.O.B.; supervision, A.V.M. and A.V.A.; funding acquisition, A.V.M. All authors have read and agreed to the published version of the manuscript.

Funding

This research was funded by Russian Scientific Foundation, grant number 23-14-00209.

Institutional Review Board Statement

Not applicable.

Informed Consent Statement

Not applicable.

Data Availability Statement

All data are available upon request.

Acknowledgments

We thank Timofei Zatsepin for conducting oligonucleotide synthesis.

Conflicts of Interest

The authors declare no conflicts of interest.

Abbreviations

The following abbreviations are used in this manuscript:
8-oxoA8-oxoadenine
8-oxoG8-oxoguanine

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Figure 1. DNA polymerase activity of PrimPol on DNA with 8-oxoA or 8-oxoG in the presence of Mg2+. (A) Primer extension reactions on DNA containing 8-oxoA or 8-oxoG with Mg2+. Reactions were carried out in the presence of 10 mM MgCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 4 min. (B) Diagram shows the percent of primer extension on DNA with 8-oxoA or 8-oxoG in reactions in the presence of Mg2+ (A). The mean values of primer extension and standard errors are indicated. (C) Diagram shows the VMAX/KM ratio calculated for DNA containing 8-oxoA or 8-oxoG in reactions in the presence of Mg2+ (Table 1).
Figure 1. DNA polymerase activity of PrimPol on DNA with 8-oxoA or 8-oxoG in the presence of Mg2+. (A) Primer extension reactions on DNA containing 8-oxoA or 8-oxoG with Mg2+. Reactions were carried out in the presence of 10 mM MgCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 4 min. (B) Diagram shows the percent of primer extension on DNA with 8-oxoA or 8-oxoG in reactions in the presence of Mg2+ (A). The mean values of primer extension and standard errors are indicated. (C) Diagram shows the VMAX/KM ratio calculated for DNA containing 8-oxoA or 8-oxoG in reactions in the presence of Mg2+ (Table 1).
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Ijms 26 06796 g002
Figure 2. DNA polymerase activity of PrimPol on DNA with 8-oxoA or 8-oxoG in the presence of Mn2+. (A) Primer extension reactions on DNA containing 8-oxoA or 8-oxoG with Mn2+. Reactions were carried out in the presence of 1 mM MnCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 1 min. (B) Diagram shows the percent of primer extension on DNA with 8-oxoA or 8-oxoG in reactions in the presence of Mn2+ (A). The mean values of primer extension and standard errors are indicated. (C) Diagram shows the VMAX/KM ratio calculated for DNA containing 8-oxoA or 8-oxoG in reactions with Mn2+ (Table 1).
Figure 2. DNA polymerase activity of PrimPol on DNA with 8-oxoA or 8-oxoG in the presence of Mn2+. (A) Primer extension reactions on DNA containing 8-oxoA or 8-oxoG with Mn2+. Reactions were carried out in the presence of 1 mM MnCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 1 min. (B) Diagram shows the percent of primer extension on DNA with 8-oxoA or 8-oxoG in reactions in the presence of Mn2+ (A). The mean values of primer extension and standard errors are indicated. (C) Diagram shows the VMAX/KM ratio calculated for DNA containing 8-oxoA or 8-oxoG in reactions with Mn2+ (Table 1).
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Figure 3. DNA polymerase activity of PrimPol on DNA with A or 8-oxoA in different sequence contexts. (A) Primer extension reactions on DNA containing A or 8-oxoA with Mg2+. DNA substrates contain A, G, T, or C at the +2 position of the template (N). Reactions were carried out in the presence of 10 mM MgCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 4 min. (C) Primer extension reactions on DNA containing A or 8-oxoA with Mn2+. DNA substrates contain A, G, T, or C at the +2 position of the template. Reactions were carried out in the presence of 1 mM MnCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 1 min. (B,D) Diagrams show the percent of primer extension on DNA with A or 8-oxoA in reactions in the presence of Mg2+ (A) and Mn2+ (C). The mean values of primer extension and standard errors are indicated.
Figure 3. DNA polymerase activity of PrimPol on DNA with A or 8-oxoA in different sequence contexts. (A) Primer extension reactions on DNA containing A or 8-oxoA with Mg2+. DNA substrates contain A, G, T, or C at the +2 position of the template (N). Reactions were carried out in the presence of 10 mM MgCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 4 min. (C) Primer extension reactions on DNA containing A or 8-oxoA with Mn2+. DNA substrates contain A, G, T, or C at the +2 position of the template. Reactions were carried out in the presence of 1 mM MnCl2, 200 nM PrimPol, 100 nM Cy5-DNA-substrate, and 200 μM of all four dNTPs (N) or individual nucleotide substrates (A—dATP; G—dGTP; T—dTTP; C—dCTP) for 1 min. (B,D) Diagrams show the percent of primer extension on DNA with A or 8-oxoA in reactions in the presence of Mg2+ (A) and Mn2+ (C). The mean values of primer extension and standard errors are indicated.
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Table 1. Steady-state kinetics analysis of dNMP incorporation opposite A, G, 8-oxoA, and 8-oxoG.
Table 1. Steady-state kinetics analysis of dNMP incorporation opposite A, G, 8-oxoA, and 8-oxoG.
TemplatedNMPVmax, % per MinKM, μMVmax/KMFinc **
Mg2+
Template AdTradio *12.9 ± 0.7420 ± 370.031 ±0.003
dT12.2 ± 0.7400 ± 420.031 ± 0.0021
dG0.4 ± 0.004184 ± 460.003 ± 0.00050.09
Template oxoAdTradio3.6 ±0.3610 ± 110.006 ±0.001
dT5.3 ± 0.1677 ± 160.008 ± 0.00011
dG0.4 ± 0.005182 ± 330.002 ± 0.00010.25
Template GdC9 ± 0.973 ± 50.123 ± 0.019
dAND ***
Template oxoGdC3.8 ± 0.3128 ± 30.029 ± 0.0041
dA2.9 ± 0.3137 ± 90.021 ± 0.00050.72
Mn2+
Template AdTradio50 ± 1.511 ± 14.5 ± 0.3
dT40 ± 0.912.2 ± 0.33.3 ± 0.011
dG2.7 ± 0.54 ± 0.30.7 ± 0.20.2
Template oxoAdTradio28 ± 1.410 ± 0.52.7 ± 0.1
dT22.5 ± 0.0214.6 ± 1.91.6 ± 0.21
dG2.4 ± 0.23.9 ± 0.80.4 ± 0.10.25
Template GdC41.5 ± 0.15.1 ± 0.28.2 ± 0.3
dAND
Template oxoGdC23.5 ± 14 ± 0.56 ± 11
dA15.9 ± 0.62.5 ± 0.36.4 ± 0.91.1
* dTradio—data calculated for 32P-labelled DNA substrate. ** Finc = Vmaxnon-complementary/KMnon-complementary/Vmaxcomplementary/KMcomplementary. *** ND—not detected.
Table 2. Oligonucleotides used in this study.
Table 2. Oligonucleotides used in this study.
OligonucleotideSequence 5′-3′
Pr18-Cy5Cy5-AGGGCAGAGTATTCTTCT
Pr18AGGGCAGAGTATTCTTCT
TemplateXATTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTATACCGCAGGCAXAGAAGAATACTCTGCCCT
TemplateXGTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTATACCGCAGGCGXAGAAGAATACTCTGCCCT
TemplateXTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTATACCGCAGGCTXAGAAGAATACTCTGCCCT
TemplateXCTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTTATACCGCAGGCCXAGAAGAATACTCTGCCCT
X = A, 8-oxoA, G, or 8-oxoG.
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Boldinova, E.O.; Kruchinin, A.A.; Kamzeeva, P.N.; Aralov, A.V.; Makarova, A.V. Accurate DNA Synthesis Across 8-Oxoadenine by Human PrimPol. Int. J. Mol. Sci. 2025, 26, 6796. https://doi.org/10.3390/ijms26146796

AMA Style

Boldinova EO, Kruchinin AA, Kamzeeva PN, Aralov AV, Makarova AV. Accurate DNA Synthesis Across 8-Oxoadenine by Human PrimPol. International Journal of Molecular Sciences. 2025; 26(14):6796. https://doi.org/10.3390/ijms26146796

Chicago/Turabian Style

Boldinova, Elizaveta O., Alexander A. Kruchinin, Polina N. Kamzeeva, Andrey V. Aralov, and Alena V. Makarova. 2025. "Accurate DNA Synthesis Across 8-Oxoadenine by Human PrimPol" International Journal of Molecular Sciences 26, no. 14: 6796. https://doi.org/10.3390/ijms26146796

APA Style

Boldinova, E. O., Kruchinin, A. A., Kamzeeva, P. N., Aralov, A. V., & Makarova, A. V. (2025). Accurate DNA Synthesis Across 8-Oxoadenine by Human PrimPol. International Journal of Molecular Sciences, 26(14), 6796. https://doi.org/10.3390/ijms26146796

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