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Protein–Protein Interactions in DNA Base Excision Repair. / Moor, N. A.; Lavrik, O. I.

In: Biochemistry (Moscow), Vol. 83, No. 4, 01.04.2018, p. 411-422.

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Moor NA, Lavrik OI. Protein–Protein Interactions in DNA Base Excision Repair. Biochemistry (Moscow). 2018 Apr 1;83(4):411-422. doi: 10.1134/S0006297918040120

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Moor, N. A. ; Lavrik, O. I. / Protein–Protein Interactions in DNA Base Excision Repair. In: Biochemistry (Moscow). 2018 ; Vol. 83, No. 4. pp. 411-422.

BibTeX

@article{b17308a9b5f8414dac5d343d5cc9d136,
title = "Protein–Protein Interactions in DNA Base Excision Repair",
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, DNA repair, protein–protein interactions",
author = "Moor, {N. A.} and Lavrik, {O. I.}",
year = "2018",
month = apr,
day = "1",
doi = "10.1134/S0006297918040120",
language = "English",
volume = "83",
pages = "411--422",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "4",

}

RIS

TY - JOUR

T1 - Protein–Protein Interactions in DNA Base Excision Repair

AU - Moor, N. A.

AU - Lavrik, O. I.

PY - 2018/4/1

Y1 - 2018/4/1

N2 - 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.

AB - 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.

KW - base excision repair

KW - DNA repair

KW - protein–protein interactions

UR - http://www.scopus.com/inward/record.url?scp=85045507168&partnerID=8YFLogxK

U2 - 10.1134/S0006297918040120

DO - 10.1134/S0006297918040120

M3 - Review article

C2 - 29626928

AN - SCOPUS:85045507168

VL - 83

SP - 411

EP - 422

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 4

ER -

ID: 12668938