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  • 1
    Publication Date: 1993-07-30
    Description: Models of DNA replication in Escherichia coli involve an asymmetric DNA polymerase complex that replicates concurrently the leading and the lagging strands of double-stranded DNA. The effect of asymmetry on mutagenesis was tested with pairs of plasmids containing the unidirectional ColE1 origin of replication and a single lesion located in the leading or lagging strand. The lesion used was the covalent adduct that the chemical carcinogen N-2-acetylaminofluorene (AAF) forms with the C-8 position of guanine. Whether SOS was induced or not, mutations arose at about a 20-fold higher frequency when the AAF adduct was located in the lagging strand than when in the leading strand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veaute, X -- Fuchs, R P -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):598-600.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite Propre de Recherche Cancerogenese et Mutagenese Moleculaire et Structurale, Institut de Biologie Moleculaire et Cellulaire Centre National de la Recherche Scientifique, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342022" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Acetylaminofluorene/metabolism/toxicity ; Base Sequence ; DNA Damage ; DNA Polymerase I/metabolism ; DNA Polymerase III/metabolism ; *DNA Replication ; DNA, Bacterial/biosynthesis/*genetics ; Escherichia coli/*genetics/metabolism ; *Frameshift Mutation ; Guanine/metabolism ; Molecular Sequence Data ; *Mutagenesis ; Plasmids
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2011-10-25
    Description: Homologous recombination is a high-fidelity DNA repair pathway. Besides a critical role in accurate chromosome segregation during meiosis, recombination functions in DNA repair and in the recovery of stalled or broken replication forks to ensure genomic stability. In contrast, inappropriate recombination contributes to genomic instability, leading to loss of heterozygosity, chromosome rearrangements and cell death. The RecA/UvsX/RadA/Rad51 family of proteins catalyses the signature reactions of recombination, homology search and DNA strand invasion. Eukaryotes also possess Rad51 paralogues, whose exact role in recombination remains to be defined. Here we show that the Saccharomyces cerevisiae Rad51 paralogues, the Rad55-Rad57 heterodimer, counteract the antirecombination activity of the Srs2 helicase. The Rad55-Rad57 heterodimer associates with the Rad51-single-stranded DNA filament, rendering it more stable than a nucleoprotein filament containing Rad51 alone. The Rad51-Rad55-Rad57 co-filament resists disruption by the Srs2 antirecombinase by blocking Srs2 translocation, involving a direct protein interaction between Rad55-Rad57 and Srs2. Our results demonstrate an unexpected role of the Rad51 paralogues in stabilizing the Rad51 filament against a biologically important antagonist, the Srs2 antirecombination helicase. The biological significance of this mechanism is indicated by a complete suppression of the ionizing radiation sensitivity of rad55 or rad57 mutants by concomitant deletion of SRS2, as expected for biological antagonists. We propose that the Rad51 presynaptic filament is a meta-stable reversible intermediate, whose assembly and disassembly is governed by the balance between Rad55-Rad57 and Srs2, providing a key regulatory mechanism controlling the initiation of homologous recombination. These data provide a paradigm for the potential function of the human RAD51 paralogues, which are known to be involved in cancer predisposition and human disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3213327/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3213327/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Jie -- Renault, Ludovic -- Veaute, Xavier -- Fabre, Francis -- Stahlberg, Henning -- Heyer, Wolf-Dietrich -- CA92267/CA/NCI NIH HHS/ -- GM58015/GM/NIGMS NIH HHS/ -- U54 GM074929/GM/NIGMS NIH HHS/ -- U54 GM074929-05/GM/NIGMS NIH HHS/ -- U54GM74929/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Oct 23;479(7372):245-8. doi: 10.1038/nature10522.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of California, Davis, Davis, California 95616-8665, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22020281" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/genetics/*metabolism ; DNA Helicases/antagonists & inhibitors/*metabolism ; DNA Repair Enzymes/genetics/*metabolism ; DNA, Single-Stranded/chemistry/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Protein Binding ; Rad51 Recombinase/chemistry/*metabolism ; Saccharomyces cerevisiae/enzymology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/antagonists & ; inhibitors/chemistry/genetics/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    ISSN: 0168-9525
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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