scholarly journals Visualize Dynamics of Chromosome Structure Formation and DNA Repair/Recombination Coupled With DNA Replication: Tight Coupled Role of DNA Replication in Chromosome Compaction and DNA Recombination

10.5772/19131 ◽  
2011 ◽  
Author(s):  
Eisuke Gotoh
Keyword(s):  
Dna Repair ◽  
Dna Replication ◽  
Structure Formation ◽  
Chromosome Structure ◽  
Dna Recombination

Role of yeast Rth1 nuclease and its homologs in mutation avoidance, DNA repair, and DNA replication

1998 ◽  
Vol 34 (1) ◽  
pp. 21-29 ◽  
Author(s):  
Robert E. Johnson ◽  
Gopala K. Kovvali ◽  
Louise Prakash ◽  
S. Prakash
Keyword(s):  
Dna Repair ◽  
Dna Replication ◽  
Mutation Avoidance

scholarly journals Opposing Roles for Two Molecular Forms of Replication Protein A in Rad51-Rad54-Mediated DNA Recombination in Plasmodium falciparum

mBio ◽  
2013 ◽  
Vol 4 (3) ◽  
Author(s):  
Anusha M. Gopalakrishnan ◽  
Nirbhay Kumar
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Antigenic Variation ◽  
Protein A ◽  
Dna Recombination ◽  
Strand Exchange ◽  
Content Type ◽  
Dna Strand Exchange ◽  
Dna Strand

ABSTRACT The bacterial RecA protein and its eukaryotic homologue Rad51 play a central role in the homologous DNA strand exchange reaction during recombination and DNA repair. Previously, our lab has shown that PfRad51, the Plasmodium falciparum homologue of Rad51, exhibited ATPase activity and promoted DNA strand exchange in vitro. In this study, we evaluated the catalytic functions of PfRad51 in the presence of putative interacting partners, especially P. falciparum homologues of Rad54 and replication protein A. PfRad54 accelerated PfRad51-mediated pairing between single-stranded DNA (ssDNA) and its homologous linear double-stranded DNA (dsDNA) in the presence of 0.5 mM CaCl2. We also present evidence that recombinant PfRPA1L protein serves the function of the bacterial homologue single-stranded binding protein (SSB) in initiating homologous pairing and strand exchange activity. More importantly, the function of PfRPA1L was negatively regulated in a dose-dependent manner by PfRPA1S, another RPA homologue in P. falciparum. Finally, we present in vivo evidence through comet assays for methyl methane sulfonate-induced DNA damage in malaria parasites and accompanying upregulation of PfRad51, PfRad54, PfRPA1L, and PfRPA1S at the level of transcript and protein needed to repair DNA damage. This study provides new insights into the role of putative Rad51-interacting proteins involved in homologous recombination and emphasizes the physiological role of DNA damage repair during the growth of parasites. IMPORTANCE Homologous recombination plays a major role in chromosomal rearrangement, and Rad51 protein, aided by several other proteins, plays a central role in DNA strand exchange reaction during recombination and DNA repair. This study reports on the characterization of the role of P. falciparum Rad51 in homologous strand exchange and DNA repair and evaluates the functional contribution of PfRad54 and PfRPA1 proteins. Data presented here provide mechanistic insights into DNA recombination and DNA damage repair mechanisms in this parasite. The importance of these research findings in future work will be to investigate if Rad51-dependent mechanisms are involved in chromosomal rearrangements during antigenic variation in P. falciparum. A prominent determinant of antigenic variation, the extraordinary ability of the parasite to rapidly change its surface molecules, is associated with var genes, and antigenic variation presents a major challenge to vaccine development.

scholarly journals Contribution of Base Excision Repair, Nucleotide Excision Repair, and DNA Recombination to Alkylation Resistance of the Fission Yeast Schizosaccharomyces pombe

2000 ◽  
Vol 182 (8) ◽  
pp. 2104-2112 ◽  
Author(s):  
Asli Memisoglu ◽  
Leona Samson
Keyword(s):  
Dna Repair ◽  
Schizosaccharomyces Pombe ◽  
Nucleotide Excision Repair ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Recombination ◽  
Nucleotide Excision ◽  
Repair Pathways ◽  
Base Excision

ABSTRACT DNA damage is unavoidable, and organisms across the evolutionary spectrum possess DNA repair pathways that are critical for cell viability and genomic stability. To understand the role of base excision repair (BER) in protecting eukaryotic cells against alkylating agents, we generated Schizosaccharomyces pombe strains mutant for the mag1 3-methyladenine DNA glycosylase gene. We report that S. pombe mag1 mutants have only a slightly increased sensitivity to methylation damage, suggesting that Mag1-initiated BER plays a surprisingly minor role in alkylation resistance in this organism. We go on to show that other DNA repair pathways play a larger role than BER in alkylation resistance. Mutations in genes involved in nucleotide excision repair (rad13) and recombinational repair (rhp51) are much more alkylation sensitive thanmag1 mutants. In addition, S. pombe mutant for the flap endonuclease rad2 gene, whose precise function in DNA repair is unclear, were also more alkylation sensitive thanmag1 mutants. Further, mag1 andrad13 interact synergistically for alkylation resistance, and mag1 and rhp51 display a surprisingly complex genetic interaction. A model for the role of BER in the generation of alkylation-induced DNA strand breaks in S. pombe is discussed.

scholarly journals The "enemies within": regions of the genome that are inherently difficult to replicate

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 666 ◽  
Author(s):  
Rahul Bhowmick ◽  
Ian D Hickson
Keyword(s):  
Dna Repair ◽  
Dna Replication ◽  
Genome Organization ◽  
Molecular Basis ◽  
Mammalian Cells ◽  
Fragile Sites ◽  
Chromosome Fragility ◽  
Valuable Role ◽  
Eukaryotic Genomes

An unusual feature of many eukaryotic genomes is the presence of regions that appear intrinsically difficult to copy during the process of DNA replication. Curiously, the location of these difficult-to-replicate regions is often conserved between species, implying a valuable role in some aspect of genome organization or maintenance. The most prominent class of these regions in mammalian cells is defined as chromosome fragile sites, which acquired their name because of a propensity to form visible gaps/breaks on otherwise-condensed chromosomes in mitosis. This fragility is particularly apparent following perturbation of DNA replication—a phenomenon often referred to as “replication stress”. Here, we review recent data on the molecular basis for chromosome fragility and the role of fragile sites in the etiology of cancer. In particular, we highlight how studies on fragile sites have provided unexpected insights into how the DNA repair machinery assists in the completion of DNA replication.

scholarly journals Investigating the role of DNA repair enzymes in DNA replication and recombination (735.3)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Clayton Speed ◽  
Claudia Wiese ◽  
Ann Parplys ◽  
J. Robert Hatherill
Keyword(s):  
Dna Repair ◽  
Dna Replication ◽  
Dna Repair Enzymes ◽  
Repair Enzymes

scholarly journals The Role of Marek’s Disease Virus UL12 and UL29 in DNA Recombination and the Virus Lifecycle

Viruses ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 111 ◽  
Author(s):  
Renato Previdelli ◽  
Luca Bertzbach ◽  
Darren Wight ◽  
Tereza Vychodil ◽  
Yu You ◽  
...  
Keyword(s):  
Dna Repair ◽  
Disease Virus ◽  
Virus Replication ◽  
Dna Recombination ◽  
Virus Genome ◽  
Marek's Disease Virus ◽  
Single Strand ◽  
Marek's Disease ◽  
Latent Virus

Marek’s disease virus (MDV) is an oncogenic alphaherpesvirus that infects chickens and integrates its genome into the telomeres of latently infected cells. MDV encodes two proteins, UL12 and UL29 (ICP8), that are conserved among herpesviruses and could facilitate virus integration. The orthologues of UL12 and UL29 in herpes simplex virus 1 (HSV-1) possess exonuclease and single strand DNA-binding activity, respectively, and facilitate DNA recombination; however, the role of both proteins in the MDV lifecycle remains elusive. To determine if UL12 and/or UL29 are involved in virus replication, we abrogated their expression in the very virulent RB-1B strain. Abrogation of either UL12 or UL29 resulted in a severe impairment of virus replication. We also demonstrated that MDV UL12 can aid in single strand annealing DNA repair, using a well-established reporter cell line. Finally, we assessed the role of UL12 and UL29 in MDV integration and maintenance of the latent virus genome. We could demonstrate that knockdown of UL12 and UL29 does not interfere with the establishment or maintenance of latency. Our data therefore shed light on the role of MDV UL12 and UL29 in MDV replication, DNA repair, and maintenance of the latent virus genome.

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