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DNA Damage and Repair in Health and Diseases
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DNA Damage and Repair in Health and Diseases

A special issue of Current Issues in Molecular Biology (ISSN 1467-3045). This special issue belongs to the section "Biochemistry, Molecular and Cellular Biology".

Deadline for manuscript submissions: 31 July 2024 | Viewed by 316

Special Issue Editor

Prof. Dr. Tomasz Popławski

E-Mail Website
Guest Editor
Department of Microbiology and Pharmaceutical Biochemistry, Medical University of Lodz, 90-136 Lodz, Poland
Interests: DNA; epigenetics; genetic analysis; cyto and genotoxicity; biochemistry; enzymes; metabolism
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In human cells, DNA lesions are formed as a result of normal cell metabolic activity and various environmental factors. These represent highly serious challenges for any cell due to the tremendous number of these incidents estimated at tens of thousands per day. Many of these lesions cause structural damage to the DNA molecule, thereby altering or eliminating the cell's ability to use DNA as a source of information; therefore, DNA repair is constantly activated in response to DNA damage. At the cellular level, DNA lesions that are not repaired correctly can lead to genome instability, apoptosis and senescence, thereby significantly affecting the development and increasing the aging process of organisms. Moreover, loss of genome integrity predisposes organisms to immune deficiencies and cancer. Therefore, it is critical that cells efficiently respond to DNA damage. DNA damage response (DDR) includes not only DNA repair, but also changes in chromatin folding, signalling of DNA lesions, coordination of their repair through checkpoints, and cell death via apoptosis or senescence. In addition, transcriptome changes and energy depletion are observed in cells with damaged DNA. DNA repair capacity is critical for the integrity of normal human function. As such, this Special Issue welcomes new research papers and timely reviews on various aspects of DNA damage response in human health and diseases.

Prof. Dr. Tomasz Popławski
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Current Issues in Molecular Biology is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • DNA damage
  • DNA repair
  • DNA repair enzymes
  • genome stability
  • oxidative damage
  • cancers
  • autoimmune diseases

Published Papers (1 paper)

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Research

14 pages, 3918 KiB  
Article
Structural and Dynamic Features of the Recognition of 8-oxoguanosine Paired with an 8-oxoG-clamp by Human 8-oxoguanine-DNA Glycosylase
by Maria V. Lukina, Polina V. Zhdanova and Vladimir V. Koval
Curr. Issues Mol. Biol. 2024, 46(5), 4119-4132; https://doi.org/10.3390/cimb46050253 - 29 Apr 2024
Viewed by 193
Abstract
8-oxoguanine (oxoG) is formed in DNA by the action of reactive oxygen species. As a highly mutagenic and the most common oxidative DNA lesion, it is an important marker of oxidative stress. Human 8-oxoguanine-DNA glycosylase (OGG1) is responsible for its prompt removal in [...] Read more.
8-oxoguanine (oxoG) is formed in DNA by the action of reactive oxygen species. As a highly mutagenic and the most common oxidative DNA lesion, it is an important marker of oxidative stress. Human 8-oxoguanine-DNA glycosylase (OGG1) is responsible for its prompt removal in human cells. OGG1 is a bifunctional DNA glycosylase with N-glycosylase and AP lyase activities. Aspects of the detailed mechanism underlying the recognition of 8-oxoguanine among numerous intact bases and its subsequent interaction with the enzyme’s active site amino acid residues are still debated. The main objective of our work was to determine the effect (structural and thermodynamic) of introducing an oxoG-clamp in model DNA substrates on the process of 8-oxoG excision by OGG1. Towards that end, we used DNA duplexes modeling OGG1-specific lesions: 8-oxoguanine or an apurinic/apyrimidinic site with either cytidine or the oxoG-clamp in the complementary strand opposite to the lesion. It was revealed that there was neither hydrolysis of the N-glycosidic bond at oxoG nor cleavage of the sugar–phosphate backbone during the reaction between OGG1 and oxoG-clamp-containing duplexes. Possible structural reasons for the absence of OGG1 enzymatic activity were studied via the stopped-flow kinetic approach and molecular dynamics simulations. The base opposite the damage was found to have a critical effect on the formation of the enzyme–substrate complex and the initiation of DNA cleavage. The oxoG-clamp residue prevented the eversion of the oxoG base into the OGG1 active site pocket and impeded the correct convergence of the apurinic/apyrimidinic site of DNA and the attacking nucleophilic group of the enzyme. An obtained three-dimensional model of the OGG1 complex with DNA containing the oxoG-clamp, together with kinetic data, allowed us to clarify the role of the contact of amino acid residues with DNA in the formation of (and rearrangements in) the enzyme–substrate complex. Full article
(This article belongs to the Special Issue DNA Damage and Repair in Health and Diseases)
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