The paper, titled “The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair,” reports new findings on how the UvrA2 protein uses its ATPase activity to probe DNA for damage lesions, such as those caused by UV radiation, and initiate nucleotide excision repair (NER). This DNA repair process corrects tens of thousands of lesions introduced daily into the human genome by UV rays and chemical agents.
Defects in NER proteins lead to increased UV sensitivity and a high risk of skin cancer, as well as the hereditary disorder Xeroderma Pigmentosum, highlighting the vital role of NER in protecting the genome and maintaining human health. Case employed ensemble kinetic methods to study the mechanism of action of UvrA2, a bacterial NER protein.
“The outcome is a new and deeper understanding of how UvrA2 works, which will help advance our knowledge of NER,” Case explained.
The research at Wesleyan University was supported by NIH grant R15 GM114743 awarded to Manju Hingorani, professor of molecular biology and biochemistry; professor, integrative sciences.
Case spoke about his research at a Graduate Speakers Series discussion in 2018.