Fate of the replisome following arrest by UV-induced DNA damage in
            <i>Escherichia coli</i>

Jeiranian, H. Arthur; Schalow, Brandy J.; Courcelle, Charmain T.; Courcelle, Justin

doi:10.1073/pnas.1300624110

Cited by 24 publications

(30 citation statements)

References 62 publications

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“…Another approach to tolerate CPD involves polymerases transiently dissociating upon encountering this lesion and allowing repair enzymes or translesion polymerases to repair or bypass this lesion. The helicase-primase complex remains bound to the template DNA and serves to maintain the integrity of the replication fork, directing the reassembled replisome to the correct location [87]. …”

Section: Bypassing Dna Damage By the Dna Replisomementioning

confidence: 99%

Mechanisms of mutagenesis: DNA replication in the presence of DNA damage

Liu

Xue

Tang

et al. 2016

Mutation Research/Reviews in Mutation Research

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Environmental mutagens cause DNA damage that disturbs replication and produces mutations, leading to cancer and other diseases. We discuss mechanisms of mutagenesis resulting from DNA damage, from the level of DNA replication by a single polymerase to the complex DNA replisome of some typical model organisms (including bacteriophage T7, T4, Sulfolobus solfataricus, E. coli, yeast and human). For a single DNA polymerase, DNA damage can affect replication in three major ways: reducing replication fidelity, causing frameshift mutations, and blocking replication. For the DNA replisome, protein interactions and the functions of accessory proteins can yield rather different results even with a single DNA polymerase. The mechanism of mutation during replication performed by the DNA replisome is a long-standing question. Using new methods and techniques, the replisomes of certain organisms and human cell extracts can now be investigated with regard to the bypass of DNA damage. In this review, we consider the molecular mechanism of mutagenesis resulting from DNA damage in replication at the levels of single DNA polymerases and complex DNA replisomes, including translesion DNA synthesis.

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Section: Bypassing Dna Damage By the Dna Replisomementioning

confidence: 99%

Mechanisms of mutagenesis: DNA replication in the presence of DNA damage

Liu

Xue

Tang

et al. 2016

Mutation Research/Reviews in Mutation Research

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“…However, multiple studies have shown empirically that recBC mutants remain able to restore replication after these challenges, and a series of studies have shown directly that RecBCD plays no role in the degradation of the nascent fork DNA at impeded replication forks [62, 106–109]. In addition, the use of 2D-agarose gels to examine arrested forks at a range of impediments in both prokaryotes and eukaryotes has shown that the replication fork DNA remains stable and intact throughout the recovery process [110–115]. Thus, despite its persistence in the literature [116–122], there is little experimental support to suggest that fork collapse occurs frequently or is a substrate for recBCD processing.…”

Section: Double-strand Breaks May Be Infrequent Eventsmentioning

confidence: 99%

RecBCD is required to complete chromosomal replication: Implications for double-strand break frequencies and repair mechanisms

et al. 2015

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Several aspects of the mechanism of homologous double strand break repair remain unclear. Although intensive efforts have focused on how recombination reactions initiate, far less is known about the molecular events that follow. Based upon biochemical studies, current models propose that RecBCD processes double strand ends and loads RecA to initiate recombinational repair. However, recent studies have shown that RecBCD plays a critical role in completing replication events on the chromosome through a mechanism that does not involve RecA or recombination. Here, we examine several studies, both early and recent, that suggest RecBCD also operates late in the recombination process- after initiation, strand invasion, and crossover resolution have occurred. Similar to its role in completing replication, we propose a model in which RecBCD is required to resect and resolve the DNA synthesis associated with homologous recombination at the point where the missing sequences on the broken molecule have been restored. We explain how the impaired ability to complete chromosome replication in recBC and recD mutants is likely to account for the loss of viability and genome instability in these mutants, and conclude that spontaneous double strand breaks and replication fork collapse occur far less frequently than previously speculated.

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“…[1] The E. coli replisome transiently stalls at leading-strand template lesionsa nd can either reinitiate replication downstream of the lesion with the aid of the primase DnaG or recruit special DNA polymerases thatc an bypass the lesion through translesion synthesis. [37] DNA polymerase IV could engage productively with the E. coli replisome to bypass leading-strand templateb ulky lesionsi ncluding CPD and THF. [38] Polymerases transiently dissociate from the DNA template upon encountering the CPD lesion.T he helicase and primase complex bound to the template DNA maintains the polymerase at the replication fork.…”

Section: Resultsmentioning

confidence: 99%

Protein Interactions in the T7 DNA Replisome Facilitate DNA Damage Bypass

et al. 2018

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The DNA replisome inevitably encounters DNA damage during DNA replication. The T7 DNA replisome contains a DNA polymerase (gp5), the processivity factor thioredoxin (trx), a helicase-primase (gp4), and a ssDNA-binding protein (gp2.5). T7 protein interactions mediate this DNA replication. However, whether the protein interactions could promote DNA damage bypass is still little addressed. In this study, we investigated strand-displacement DNA synthesis past 8-oxoG or O -MeG lesions at the synthetic DNA fork by the T7 DNA replisome. DNA damage does not obviously affect the binding affinities between helicase, polymerase, and DNA fork. Relative to unmodified G, both 8-oxoG and O -MeG-as well as GC-rich template sequence clusters-inhibit strand-displacement DNA synthesis and produce partial extension products. Relative to the gp4 ΔC-tail, gp4 promotes DNA damage bypass. The presence of gp2.5 also promotes it. Thus, the interactions of polymerase with helicase and ssDNA-binding protein facilitate DNA damage bypass. Accessory proteins in other complicated DNA replisomes also facilitate bypassing DNA damage in similar manner. This work provides new mechanistic information relating to DNA damage bypass by the DNA replisome.

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Fate of the replisome following arrest by UV-induced DNA damage in Escherichia coli

Cited by 24 publications

References 62 publications

Mechanisms of mutagenesis: DNA replication in the presence of DNA damage

Mechanisms of mutagenesis: DNA replication in the presence of DNA damage

RecBCD is required to complete chromosomal replication: Implications for double-strand break frequencies and repair mechanisms

Protein Interactions in the T7 DNA Replisome Facilitate DNA Damage Bypass

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