scholarly journals Aflatoxin B1-Induced Developmental and DNA Damage in Caenorhabditis elegans

Toxins ◽  
2016 ◽  
Vol 9 (1) ◽  
pp. 9 ◽  
Author(s):  
Wei-Hong Feng ◽  
Kathy Xue ◽  
Lili Tang ◽  
Phillip Williams ◽  
Jia-Sheng Wang
BIO-PROTOCOL ◽  
2015 ◽  
Vol 5 (11) ◽  
Author(s):  
Hyun-Min Kim ◽  
Monica Colai�covo

Chemosphere ◽  
2014 ◽  
Vol 108 ◽  
pp. 231-238 ◽  
Author(s):  
Yun Wang ◽  
Shunchang Wang ◽  
Xun Luo ◽  
Yanan Yang ◽  
Fenglei Jian ◽  
...  

Gerontology ◽  
2015 ◽  
Vol 62 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Jin-Sun Ryu ◽  
Hyeon-Sook Koo

Werner syndrome protein (WRN) is unusual among RecQ family DNA helicases in having an additional exonuclease activity. WRN is involved in the repair of double-strand DNA breaks via the homologous recombination and nonhomologous end joining pathways, and also in the base excision repair pathway. In addition, the protein promotes the recovery of stalled replication forks. The helicase activity is thought to unwind DNA duplexes, thereby moving replication forks or Holliday junctions. The targets of the exonuclease could be the nascent DNA strands at a replication fork or the ends of double-strand DNA breaks. However, it is not clear which enzyme activities are essential for repairing different types of DNA damage. Model organisms such as mice, flies, and worms deficient in WRN homologs have been investigated to understand the physiological results of defects in WRN activity. Premature aging, the most remarkable characteristic of Werner syndrome, is also seen in the mutant mice and worms, and hypersensitivity to DNA damage has been observed in WRN mutants of all three model organisms, pointing to conservation of the functions of WRN. In the nematode Caenorhabditis elegans, the WRN homolog contains a helicase domain but no exonuclease domain, so that this animal is very useful for studying the in vivo functions of the helicase without interference from the activity of the exonuclease. Here, we review the current status of investigations of C. elegans WRN-1 and discuss its functional differences from the mammalian homologs.


DNA Repair ◽  
2012 ◽  
Vol 11 (11) ◽  
pp. 857-863 ◽  
Author(s):  
Senyene E. Hunter ◽  
Margaret A. Gustafson ◽  
Kathleen M. Margillo ◽  
Sean A. Lee ◽  
Ian T. Ryde ◽  
...  

2018 ◽  
Vol 26 ◽  
pp. 42-48 ◽  
Author(s):  
Grace A. Odongo ◽  
Nina Schlotz ◽  
Susanne Baldermann ◽  
Susanne Neugart ◽  
Benard Ngwene ◽  
...  

Author(s):  
Franziska Ferk ◽  
Karl Speer ◽  
Miroslav Mišík ◽  
Armen Nersesyan ◽  
Siegfried Knasmüller

2014 ◽  
Vol 86 (16) ◽  
pp. 8418-8424 ◽  
Author(s):  
Ian M. Huffnagle ◽  
Alyssa Joyner ◽  
Blake Rumble ◽  
Sherif Hysa ◽  
David Rudel ◽  
...  

2017 ◽  
Vol 157 (2) ◽  
pp. 510-518 ◽  
Author(s):  
Xinyue You ◽  
Jing Xi ◽  
Yiyi Cao ◽  
Jinfu Zhang ◽  
Yang Luan

2020 ◽  
Vol 10 (11) ◽  
pp. 3929-3947
Author(s):  
Nick St. John ◽  
Julian Freedland ◽  
Henri Baldino ◽  
Francis Doyle ◽  
Cinzia Cera ◽  
...  

Exposure to the mycotoxin aflatoxin B1 (AFB1) strongly correlates with hepatocellular carcinoma (HCC). P450 enzymes convert AFB1 into a highly reactive epoxide that forms unstable 8,9-dihydro-8-(N7-guanyl)-9-hydroxyaflatoxin B1 (AFB1-N7-Gua) DNA adducts, which convert to stable mutagenic AFB1 formamidopyrimidine (FAPY) DNA adducts. In CYP1A2-expressing budding yeast, AFB1 is a weak mutagen but a potent recombinagen. However, few genes have been identified that confer AFB1 resistance. Here, we profiled the yeast genome for AFB1 resistance. We introduced the human CYP1A2 into ∼90% of the diploid deletion library, and pooled samples from CYP1A2-expressing libraries and the original library were exposed to 50 μM AFB1 for 20 hs. By using next generation sequencing (NGS) to count molecular barcodes, we initially identified 86 genes from the CYP1A2-expressing libraries, of which 79 were confirmed to confer AFB1 resistance. While functionally diverse genes, including those that function in proteolysis, actin reorganization, and tRNA modification, were identified, those that function in postreplication DNA repair and encode proteins that bind to DNA damage were over-represented, compared to the yeast genome, at large. DNA metabolism genes also included those functioning in checkpoint recovery and replication fork maintenance, emphasizing the potency of the mycotoxin to trigger replication stress. Among genes involved in postreplication repair, we observed that CSM2, a member of the CSM2(SHU) complex, functioned in AFB1-associated sister chromatid recombination while suppressing AFB1-associated mutations. These studies thus broaden the number of AFB1 resistance genes and have elucidated a mechanism of error-free bypass of AFB1-associated DNA adducts.


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