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Kinetic Aspects of Enzyme-Mediated Repair of DNA Single-Strand Breaks Full article

Journal Biosystems
ISSN: 0303-2647 , E-ISSN: 1872-8324
Output data Year: 2016, Volume: 150, Pages: 194-199 Pages count : 6 DOI: 10.1016/j.biosystems.2016.09.007
Tags DNA damage and repair, Gap filling, Ligation, Mean-field kinetic equations, Processing of damaged ends, Random coil model
Authors Zhdanov Vladimir P. 1,2
Affiliations
1 Division of Biological Physics, Department of Physics, Chalmers University of Technology, S-41296 Göteborg, Sweden
2 Boreskov Institute of Catalysis, Russian Academy of Sciences, Novosibirsk 630090, Russia

Funding (1)

1 Swedish Research Council 2013-7421

Abstract: In cells and bacteria, DNA can be damaged in different ways. The efficient damage repair, mediated by various enzymes, is crucial for their survival. Most frequently, the damage is reduced to single-strand breaks. In human cells, according to the experiments, the repair of such breaks can mechanistically be divided into four steps including (i) the break detection, (ii) processing of damaged ends, (iii) gap filling, and (iv) ligation of unbound ends of the broken strand. The first and second steps run in parallel while the third and fourth steps are sequential. The author proposes a kinetic model describing these steps. It allows one to understand the likely dependence of the number of breaks in different states on enzyme concentrations. The dependence of these concentrations on the rate of the formation of breaks can be understood as well. In addition, the likely role of unzipping and zipping of the fragments of broken ends of the strand in the ligation step has been scrutinized taking the specifics of binding of DNA stands into account.
Cite: Zhdanov V.P.
Kinetic Aspects of Enzyme-Mediated Repair of DNA Single-Strand Breaks
Biosystems. 2016. V.150. P.194-199. DOI: 10.1016/j.biosystems.2016.09.007 WOS Scopus РИНЦ AN PMID OpenAlex
Dates:
Submitted: Jul 29, 2016
Accepted: Sep 23, 2016
Published online: Oct 19, 2016
Published print: Dec 1, 2016
Identifiers:
Web of science: WOS:000390631700021
Scopus: 2-s2.0-84993995662
Elibrary: 27581838
Chemical Abstracts: 2016:1802559
PMID: 27771386
OpenAlex: W2535615068
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