3-Methyladenine DNA glycosylase is important for cellular resistance to psoralen interstrand cross-links

Maor-Shoshani, Ayelet; Meira, Lisiane B.; Xiong, Yijun; Samson, Leona D.

doi:10.1016/j.dnarep.2008.04.017

Cited by 14 publications

(19 citation statements)

References 57 publications

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“…These results indicate that the influence of the sequence context affects both insertion opposite the THF and extension beyond the mismatch, as has been shown for other polymerases (45,46). Importantly, the bypass efficiency of B35DNAP is higher than that of other replicative polymerases, such as yeast pole (6-17%) (46), and comparable to previously reported values for Y family polymerases, including human DNA polymerase η (10-13%), Sulfolobus solfataricus Dpo4 (13-30%), and Escherichia coli DNA polymerase IV (25-40%) (45,47,48).…”

Section: Resultssupporting

confidence: 72%

DNA polymerase from temperate phage Bam35 is endowed with processive polymerization and abasic sites translesion synthesis capacity

Berjón-Otero

Villar

Vega

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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DNA polymerases (DNAPs) responsible for genome replication are highly faithful enzymes that nonetheless cannot deal with damaged DNA. In contrast, translesion synthesis (TLS) DNAPs are suitable for replicating modified template bases, although resulting in very lowfidelity products. Here we report the biochemical characterization of the temperate bacteriophage Bam35 DNA polymerase (B35DNAP), which belongs to the protein-primed subgroup of family B DNAPs, along with phage Φ29 and other viral and mobile element polymerases. B35DNAP is a highly faithful DNAP that can couple strand displacement to processive DNA synthesis. These properties allow it to perform multiple displacement amplification of plasmid DNA with a very low error rate. Despite its fidelity and proofreading activity, B35DNAP was able to successfully perform abasic site TLS without template realignment and inserting preferably an A opposite the abasic site (A rule). Moreover, deletion of the TPR2 subdomain, required for processivity, impaired primer extension beyond the abasic site. Taken together, these findings suggest that B35DNAP may perform faithful and processive genome replication in vivo and, when required, TLS of abasic sites.protein-primed DNA polymerase | Bam35 | abasic sites | translesion synthesis | isothermal DNA amplification R eplicative DNA polymerases (DNAPs) from A and B families, collectively termed replicases, exhibit a "tight fit" for their DNA and dNTP substrates and are wondrously adapted to form correct Watson-Crick base pairs, resulting in very pronounced fidelity (1, 2). This strict preference to produce A:T and G:C base pairs is also the Achilles heel of faithful DNA polymerases, however, because they are strongly inhibited by modified nucleotides present at sites of DNA damage, leading to the stalling of replication fork and eventually to replicative stress and cell death (3). At the stalled replication fork, the DNA polymerase may be exchanged by a translesion synthesis (TLS) polymerase, generally belonging to the Y family. These enzymes possess looser solventexposed active sites, which allows them to deal with aberrant DNA features much better, although with a very low polymerization accuracy with the risk of the accumulation of mutations and genetic instability (4, 5). Alternatively, nonbulky modified bases, such as uracil and 8-oxo-deoxyguanosine (8oxoG), can be bypassed by replicases, with faithful or mutagenic outcomes that can be modified by the sequence context and dNTP availability (6, 7).Abasic or apurinic/apyrimidinic (AP) sites are the most common DNA lesions arising in cells when the N-glycosydic bond between the sugar moiety and the nucleobase is broken, either spontaneously or by a DNA glycosylase reaction product in the base excision repair pathway (8, 9). Unrepaired abasic sites are highly blocking lesions for replicative DNA polymerases (10), although mutant polymerases with impaired proofreading activity or with mutations in the polymerization active site residues that affect the incoming nucleotide sel...

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Section: Resultssupporting

confidence: 72%

DNA polymerase from temperate phage Bam35 is endowed with processive polymerization and abasic sites translesion synthesis capacity

Berjón-Otero

Villar

Vega

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…Whether or not this increased sensitivity was the result of impaired removal of interstrand crosslinks or one of the many monoadducts formed by these compounds, however, was not determined. More recent data from the Samson laboratory indicate that MPG (also known as AAG) is important for resistance of mouse embryonic stem cells to psoralen-induced interstrand crosslinks, but not angelicin-induced monoadducts, although the exact molecular process that engages MPG has not been elucidated (9).…”

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confidence: 99%

NEIL1 Responds and Binds to Psoralen-induced DNA Interstrand Crosslinks

McNeill

Paramasivam

Baldwin

et al. 2013

Journal of Biological Chemistry

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Background: Components of base excision repair participate in the processing of psoralen-induced DNA adducts. Results: NEIL1 glycosylase responds and binds to psoralen interstrand crosslinks, and interferes with efficient recognition and removal of these lesions. Conclusion: NEIL1 exhibits affinity for DNA interstrand crosslinks and regulates crosslink processing. Significance: Besides the efficiency of the canonical pathways, the abundance and composition of NEIL1 may influence responsiveness to environmental and therapeutic DNA crosslinking agents.

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“…In 2007, CouvePrivat et al declared that HeLa cells lacking BER proteins human apurinic/apyrimidinic endonuclease (APE1) and/or DNA glycosylase NEIL1 (glycosylases initiating the first step in base excision repair) become hypersensitive to 8-methoxypsoralen after UVA exposure [82]. Somewhat later, it was reported that cells lacking MPG are hypersensitive to cross-linking [83]. In 2009 Zhu et al identified the role of XRCC1 protein, which also represents BER protein family, in binding to cisplatin-DNA ICL [84].…”

Section: Mechanisms Involved In Icl Repairingmentioning

confidence: 98%

DNA Interstrand Cross-Linking Agents and their Chemotherapeutic Potential

Brulíková

Hlaváč²,

Hradil

2012

CMC

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DNA interstrand cross-linking (ICL) agents are an important group of cytotoxic drugs with the capability of binding covalently between two strands of DNA, thereby preventing vital processes such as replication or transcription in dividing cells. In anticancer therapy however, their potential is limited due to the resistance by various mechanisms. In order to develop highly effective antitumor drugs it is necessary to study both effective ICL formations and their subsequent repair mechanisms. This review presents an overview of development over the past decade and the use of both well-known and new DNA interstrand cross-linking agents. Their potential in applications especially as anticancer chemotherapeutics in the framework of current knowledge of repair mechanisms and development of combined chemotherapy is discussed.

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3-Methyladenine DNA glycosylase is important for cellular resistance to psoralen interstrand cross-links

Cited by 14 publications

References 57 publications

DNA polymerase from temperate phage Bam35 is endowed with processive polymerization and abasic sites translesion synthesis capacity

DNA polymerase from temperate phage Bam35 is endowed with processive polymerization and abasic sites translesion synthesis capacity

NEIL1 Responds and Binds to Psoralen-induced DNA Interstrand Crosslinks

DNA Interstrand Cross-Linking Agents and their Chemotherapeutic Potential

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