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The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates. / Bakman, Artemiy S; Boichenko, Stanislav S; Kuznetsova, Aleksandra A et al.

In: International Journal of Molecular Sciences, Vol. 24, No. 11, 9594, 31.05.2023.

Research output: Contribution to journalArticlepeer-review

Harvard

Bakman, AS, Boichenko, SS, Kuznetsova, AA, Ishchenko, AA, Saparbaev, M & Kuznetsov, NA 2023, 'The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates', International Journal of Molecular Sciences, vol. 24, no. 11, 9594. https://doi.org/10.3390/ijms24119594

APA

Bakman, A. S., Boichenko, S. S., Kuznetsova, A. A., Ishchenko, A. A., Saparbaev, M., & Kuznetsov, N. A. (2023). The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates. International Journal of Molecular Sciences, 24(11), [9594]. https://doi.org/10.3390/ijms24119594

Vancouver

Bakman AS, Boichenko SS, Kuznetsova AA, Ishchenko AA, Saparbaev M, Kuznetsov NA. The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates. International Journal of Molecular Sciences. 2023 May 31;24(11):9594. doi: 10.3390/ijms24119594

Author

Bakman, Artemiy S ; Boichenko, Stanislav S ; Kuznetsova, Aleksandra A et al. / The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates. In: International Journal of Molecular Sciences. 2023 ; Vol. 24, No. 11.

BibTeX

@article{1133d0ed832e4c99a04265c395177a40,
title = "The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates",
abstract = "Base excision repair (BER) is one of the important systems for the maintenance of genome stability via repair of DNA lesions. BER is a multistep process involving a number of enzymes, including damage-specific DNA glycosylases, apurinic/apyrimidinic (AP) endonuclease 1, DNA polymerase β, and DNA ligase. Coordination of BER is implemented by multiple protein-protein interactions between BER participants. Nonetheless, mechanisms of these interactions and their roles in the BER coordination are poorly understood. Here, we report a study on Polβ's nucleotidyl transferase activity toward different DNA substrates (that mimic DNA intermediates arising during BER) in the presence of various DNA glycosylases (AAG, OGG1, NTHL1, MBD4, UNG, or SMUG1) using rapid-quench-flow and stopped-flow fluorescence approaches. It was shown that Polβ efficiently adds a single nucleotide into different types of single-strand breaks either with or without a 5'-dRP-mimicking group. The obtained data indicate that DNA glycosylases AAG, OGG1, NTHL1, MBD4, UNG, and SMUG1, but not NEIL1, enhance Polβ's activity toward the model DNA intermediates.",
keywords = "Humans, DNA Polymerase beta/metabolism, DNA Repair, DNA-(Apurinic or Apyrimidinic Site) Lyase/metabolism, DNA Glycosylases/metabolism, DNA Replication, DNA, DNA Damage",
author = "Bakman, {Artemiy S} and Boichenko, {Stanislav S} and Kuznetsova, {Aleksandra A} and Ishchenko, {Alexander A} and Murat Saparbaev and Kuznetsov, {Nikita A}",
note = "Funding: This work was supported by the Ministry of Science and Higher Education of the Russian Federation, agreement No. 075-15-2021-1085.",
year = "2023",
month = may,
day = "31",
doi = "10.3390/ijms24119594",
language = "English",
volume = "24",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "11",

}

RIS

TY - JOUR

T1 - The Impact of Human DNA Glycosylases on the Activity of DNA Polymerase β toward Various Base Excision Repair Intermediates

AU - Bakman, Artemiy S

AU - Boichenko, Stanislav S

AU - Kuznetsova, Aleksandra A

AU - Ishchenko, Alexander A

AU - Saparbaev, Murat

AU - Kuznetsov, Nikita A

N1 - Funding: This work was supported by the Ministry of Science and Higher Education of the Russian Federation, agreement No. 075-15-2021-1085.

PY - 2023/5/31

Y1 - 2023/5/31

N2 - Base excision repair (BER) is one of the important systems for the maintenance of genome stability via repair of DNA lesions. BER is a multistep process involving a number of enzymes, including damage-specific DNA glycosylases, apurinic/apyrimidinic (AP) endonuclease 1, DNA polymerase β, and DNA ligase. Coordination of BER is implemented by multiple protein-protein interactions between BER participants. Nonetheless, mechanisms of these interactions and their roles in the BER coordination are poorly understood. Here, we report a study on Polβ's nucleotidyl transferase activity toward different DNA substrates (that mimic DNA intermediates arising during BER) in the presence of various DNA glycosylases (AAG, OGG1, NTHL1, MBD4, UNG, or SMUG1) using rapid-quench-flow and stopped-flow fluorescence approaches. It was shown that Polβ efficiently adds a single nucleotide into different types of single-strand breaks either with or without a 5'-dRP-mimicking group. The obtained data indicate that DNA glycosylases AAG, OGG1, NTHL1, MBD4, UNG, and SMUG1, but not NEIL1, enhance Polβ's activity toward the model DNA intermediates.

AB - Base excision repair (BER) is one of the important systems for the maintenance of genome stability via repair of DNA lesions. BER is a multistep process involving a number of enzymes, including damage-specific DNA glycosylases, apurinic/apyrimidinic (AP) endonuclease 1, DNA polymerase β, and DNA ligase. Coordination of BER is implemented by multiple protein-protein interactions between BER participants. Nonetheless, mechanisms of these interactions and their roles in the BER coordination are poorly understood. Here, we report a study on Polβ's nucleotidyl transferase activity toward different DNA substrates (that mimic DNA intermediates arising during BER) in the presence of various DNA glycosylases (AAG, OGG1, NTHL1, MBD4, UNG, or SMUG1) using rapid-quench-flow and stopped-flow fluorescence approaches. It was shown that Polβ efficiently adds a single nucleotide into different types of single-strand breaks either with or without a 5'-dRP-mimicking group. The obtained data indicate that DNA glycosylases AAG, OGG1, NTHL1, MBD4, UNG, and SMUG1, but not NEIL1, enhance Polβ's activity toward the model DNA intermediates.

KW - Humans

KW - DNA Polymerase beta/metabolism

KW - DNA Repair

KW - DNA-(Apurinic or Apyrimidinic Site) Lyase/metabolism

KW - DNA Glycosylases/metabolism

KW - DNA Replication

KW - DNA

KW - DNA Damage

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85161520985&origin=inward&txGid=6c0524998881990c4b5ba993b451af39

U2 - 10.3390/ijms24119594

DO - 10.3390/ijms24119594

M3 - Article

C2 - 37298543

VL - 24

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 11

M1 - 9594

ER -

ID: 52329914