Biochemistry (Moscow)

, Volume 83, Issue 4, pp 411–422 | Cite as

Protein–Protein Interactions in DNA Base Excision Repair

Review
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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.

Keywords

base excision repair protein–protein interactions DNA repair 

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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Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  1. 1.Institute of Chemical Biology and Fundamental MedicineSiberian Branch of the Russian Academy of SciencesNovosibirskRussia
  2. 2.Novosibirsk State UniversityNovosibirskRussia

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