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REVIEW: Post-translational Modifications of Nucleotide Excision Repair Proteins and Their Role in the DNA Repair

N. I. Rechkunova1,2,a*, E. A. Maltseva1, and O. I. Lavrik1,2

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

2Novosibirsk State University, 630090 Novosibirsk, Russia

* To whom correspondence should be addressed.

Received March 21, 2019; Revised April 26, 2019; Accepted May 15, 2019
Nucleotide excision repair (NER) is one of the major DNA repair pathways aimed at maintaining genome stability. Correction of DNA damage by the NER system is a multistage process that proceeds with the formation of multiple DNA–protein and protein–protein intermediate complexes and requires precise coordination and regulation. NER proteins undergo post-translational modifications, such as ubiquitination, sumoylation, phosphorylation, acetylation, and poly(ADP-ribosyl)ation. These modifications affect the interaction of NER factors with DNA and other proteins and thus regulate either their recruitment into the complexes or dissociation from these complexes at certain stages of DNA repair, as well as modulate the functional activity of NER proteins and control the process of DNA repair in general. Here, we review the data on the post-translational modifications of NER factors and their effects on DNA repair. Protein poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 and its impact on NER are discussed in detail, since such analysis has not been done before.
KEY WORDS: nucleotide excision repair factors, post-translational modification of proteins, activity regulation

DOI: 10.1134/S0006297919090037