Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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 и др.
в: International Journal of Molecular Sciences, Том 24, № 11, 9594, 31.05.2023.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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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