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      DNA Damage Tolerance by Eukaryotic DNA Polymerase and Primase PrimPol

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          Abstract

          PrimPol is a human deoxyribonucleic acid (DNA) polymerase that also possesses primase activity and is involved in DNA damage tolerance, the prevention of genome instability and mitochondrial DNA maintenance. In this review, we focus on recent advances in biochemical and crystallographic studies of PrimPol, as well as in identification of new protein-protein interaction partners. Furthermore, we discuss the possible functions of PrimPol in both the nucleus and the mitochondria.

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          DNA base damage by reactive oxygen species, oxidizing agents, and UV radiation.

          Jean Scotty Cadet, J Wagner (2013)
          Emphasis has been placed in this article dedicated to DNA damage on recent aspects of the formation and measurement of oxidatively generated damage in cellular DNA in order to provide a comprehensive and updated survey. This includes single pyrimidine and purine base lesions, intrastrand cross-links, purine 5',8-cyclonucleosides, DNA-protein adducts and interstrand cross-links formed by the reactions of either the nucleobases or the 2-deoxyribose moiety with the hydroxyl radical, one-electron oxidants, singlet oxygen, and hypochlorous acid. In addition, recent information concerning the mechanisms of formation, individual measurement, and repair-rate assessment of bipyrimidine photoproducts in isolated cells and human skin upon exposure to UVB radiation, UVA photons, or solar simulated light is critically reviewed.
          Article 0 comments Cited 237 times – based on 0 reviews     Review now
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            PCNA: structure, functions and interactions.

            Z Kelman (1997)
            Proliferating cell nuclear antigen (PCNA) plays an essential role in nucleic acid metabolism as a component of the replication and repair machinery. This toroidal-shaped protein encircles DNA and can slide bidirectionally along the duplex. One of the well-established functions for PCNA is its role as the processivity factor for DNA polymerase delta and epsilon. PCNA tethers the polymerase catalytic unit to the DNA template for rapid and processive DNA synthesis. In the last several years it has become apparent that PCNA interacts with proteins involved in cell-cycle progression which are not a part of the DNA polymerase apparatus. Some of these interactions have a direct effect on DNA synthesis while the roles of several other interactions are not fully understood. This review summarizes the structural features of PCNA and describes the diverse functions played by the protein in DNA replication and repair as well as its possible role in chromatin assembly and gene transcription. The PCNA interactions with different cellular proteins and the importance of these interactions are also discussed.
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              Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members

              Lakshminarayan M. Iyer, Eugene V. Koonin, Detlef Leipe … (2005)
              We report an in-depth computational study of the protein sequences and structures of the superfamily of archaeo-eukaryotic primases (AEPs). This analysis greatly expands the range of diversity of the AEPs and reveals the unique active site shared by all members of this superfamily. In particular, it is shown that eukaryotic nucleo-cytoplasmic large DNA viruses, including poxviruses, asfarviruses, iridoviruses, phycodnaviruses and the mimivirus, encode AEPs of a distinct family, which also includes the herpesvirus primases whose relationship to AEPs has not been recognized previously. Many eukaryotic genomes, including chordates and plants, encode previously uncharacterized homologs of these predicted viral primases, which might be involved in novel DNA repair pathways. At a deeper level of evolutionary connections, structural comparisons indicate that AEPs, the nucleases involved in the initiation of rolling circle replication in plasmids and viruses, and origin-binding domains of papilloma and polyoma viruses evolved from a common ancestral protein that might have been involved in a protein-priming mechanism of initiation of DNA replication. Contextual analysis of multidomain protein architectures and gene neighborhoods in prokaryotes and viruses reveals remarkable parallels between AEPs and the unrelated DnaG-type primases, in particular, tight associations with the same repertoire of helicases. These observations point to a functional equivalence of the two classes of primases, which seem to have repeatedly displaced each other in various extrachromosomal replicons.
              Article 0 comments Cited 124 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 21 July 2017
                Publication date Collection: July 2017
                Volume: 18
                Issue: 7
                Electronic Location Identifier: 1584
                Affiliations
                [1 ]Institute of Molecular Genetics of Russian Academy of Sciences, Kurchatov sq. 2, 123182 Moscow, Russia; lizaboldinova@ 123456yandex.ru (E.O.B.); shilkinevgeniy.chem@ 123456gmail.com (E.S.S.)
                [2 ]Department of Medical Biochemistry and Biophysics, Umeå University, 901 87 Umeå, Sweden; paulina.wanrooij@ 123456umu.se
                Author notes
                [* ]Correspondence: sjoerd.wanrooij@ 123456umu.se (S.W.); amakarova-img@ 123456yandex.ru (A.V.M.); Tel.: +46-72-246-03-09 (S.W.); +7-499-196-00-15 (A.V.M.)
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0002-8607-7564
                https://orcid.org/0000-0002-6513-892X
                Article
                Publisher ID: ijms-18-01584
                DOI: 10.3390/ijms18071584
                PMC ID: 5536071
                PubMed ID: 28754021
                SO-VID: 29386653-0480-43a5-8917-65cc351298a2
                Copyright © © 2017 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 26 June 2017
                Date accepted : 16 July 2017
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: primpol,replication,dna damage,mitochondria
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: primpol, replication, dna damage, mitochondria

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