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Molecular Mechanism of DNA Replication and Repair, 3rd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Genetics and Genomics".

Deadline for manuscript submissions: 31 August 2024 | Viewed by 330

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Special Issue Information

Dear Colleagues,

During cell division, the replisome machinery is capable of quickly and accurately copying billions of DNA bases in order to maintain genome integrity and prevent diseases. Nevertheless, it can produce errors, particularly when the DNA is damaged. dsDNA is a stable, chemically inert molecule that is continuously subjected to a variety of exogenous and endogenous insults throughout the cell cycle. Unrepaired or misrepaired DNA lesions may cause mutations or chromosomal damage and, ultimately, abnormalities, including oncogenic transformation. For the maintenance of genomic stability, organisms have developed signal pathways that give rise to a DNA damage response (DDR). This mechanism is characterized by its capability to tolerate DNA damage and structural impediments during DNA synthesis; thus, it replicates fork progression and stability in the presence of blocking structures or DNA lesions. Malfunctioning DDR can cause fork arrest and eventually fork collapse, leading to the formation of DNA double-strand breaks.

This Special Issue of IJMS aims to expand our current understanding of molecular and cellular mechanisms of DNA replication and repair. We want to offer a platform for high-quality publications on various aspects of DNA replication and repair research. Bringing together different aspects into one Special Issue, hopefully, will trigger the development of new therapies in human diseases.

Dr. Mariarita De Felice
Dr. Mariarosaria De Falco
Guest Editors

Manuscript Submission Information

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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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • genome stability
  • DNA repair
  • DNA replication
  • DDR

Published Papers (1 paper)

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Research

19 pages, 6159 KiB  
Article
The Impact of SNP-Induced Amino Acid Substitutions L19P and G66R in the dRP-Lyase Domain of Human DNA Polymerase β on Enzyme Activities
by Olga A. Kladova, Timofey E. Tyugashev, Denis V. Yakimov, Elena S. Mikushina, Daria S. Novopashina, Nikita A. Kuznetsov and Aleksandra A. Kuznetsova
Int. J. Mol. Sci. 2024, 25(8), 4182; https://doi.org/10.3390/ijms25084182 - 10 Apr 2024
Viewed by 238
Abstract
Base excision repair (BER), which involves the sequential activity of DNA glycosylases, apurinic/apyrimidinic endonucleases, DNA polymerases, and DNA ligases, is one of the enzymatic systems that preserve the integrity of the genome. Normal BER is effective, but due to single-nucleotide polymorphisms (SNPs), the [...] Read more.
Base excision repair (BER), which involves the sequential activity of DNA glycosylases, apurinic/apyrimidinic endonucleases, DNA polymerases, and DNA ligases, is one of the enzymatic systems that preserve the integrity of the genome. Normal BER is effective, but due to single-nucleotide polymorphisms (SNPs), the enzymes themselves—whose main function is to identify and eliminate damaged bases—can undergo amino acid changes. One of the enzymes in BER is DNA polymerase β (Polβ), whose function is to fill gaps in DNA. SNPs can significantly affect the catalytic activity of an enzyme by causing an amino acid substitution. In this work, pre-steady-state kinetic analyses and molecular dynamics simulations were used to examine the activity of naturally occurring variants of Polβ that have the substitutions L19P and G66R in the dRP-lyase domain. Despite the substantial distance between the dRP-lyase domain and the nucleotidyltransferase active site, it was found that the capacity to form a complex with DNA and with an incoming dNTP is significantly altered by these substitutions. Therefore, the lower activity of the tested polymorphic variants may be associated with a greater number of unrepaired DNA lesions. Full article
(This article belongs to the Special Issue Molecular Mechanism of DNA Replication and Repair, 3rd Edition)
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