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Protein–Protein Interactions in DNA Base Excision Repair

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Abstract

The system of base excision repair (BER) ensures correction of the most abundant DNA damages in mammalian cells and plays an important role in maintaining genome stability. Enzymes and protein factors participate in the multistage BER in a coordinated fashion, which ensures repair efficiency. The suggested coordination mechanisms are based on formation of protein complexes stabilized via either direct or indirect DNA-mediated interactions. The results of investigation of direct interactions of the proteins participating in BER with each other and with other proteins are outlined in this review. The known protein partners and sites responsible for their interaction are presented for the main participants as well as quantitative characteristics of their affinity. Information on the mechanisms of regulation of protein–protein interactions mediated by DNA intermediates and posttranslational modification is presented. It can be suggested based on all available data that the multiprotein complexes are formed on chromatin independent of the DNA damage with the help of key regulators of the BER process – scaffold protein XRCC1 and poly(ADP-ribose) polymerase 1. The composition of multiprotein complexes changes dynamically depending on the DNA damage and the stage of BER process.

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Abbreviations

AP site:

apurinic/apyrimidinic site

APE1:

AP endonuclease 1

APTX:

aprataxin

BER:

base excision repair

DNALigI/DNALigIIIα:

DNA ligase I/IIIα

dRp:

deoxyribose phosphate

FAM:

5(6)-carboxyfluorescein

FEN1:

flap endonuclease 1

FRET:

Förster resonance energy transfer

HR:

homologous recombination

MMR:

mismatch repair

NER:

nucleotide excision repair

NHEJ:

nonhomologous end joining

PAR:

poly(ADP-ribose)

PARP1/PARP2:

poly(ADP-ribose) polymerase 1/2

PNKP:

polynucleotide kinase/phosphatase

Polβ/Polδ/Polε:

DNA polymerase β/δ/ε

PTM:

posttranslational modification

TDP1:

tyrosyl-DNA phosphodiesterase 1

TMR:

5(6)-carboxytetramethylrhodamine

XRD:

X-ray diffraction analysis

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Authors and Affiliations

  1. Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090, Novosibirsk, Russia

    N. A. Moor & O. I. Lavrik

  2. Novosibirsk State University, 630090, Novosibirsk, Russia

    O. I. Lavrik

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  1. N. A. Moor
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  2. O. I. Lavrik
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Correspondence to O. I. Lavrik.

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Original Russian Text © N. A. Moor, O. I. Lavrik, 2018, published in Biokhimiya, 2018, Vol. 83, No. 4, pp. 564–576.

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Moor, N.A., Lavrik, O.I. Protein–Protein Interactions in DNA Base Excision Repair. Biochemistry Moscow 83, 411–422 (2018). https://doi.org/10.1134/S0006297918040120

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  • DOI: https://doi.org/10.1134/S0006297918040120

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