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.
Keywords
base excision repair protein–protein interactions DNA repairAbbreviations
- 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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References
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