New research has revealed the function of a widely shared enzyme component, the Zf-GRF domain, as a critical molecular tool necessary for manipulating DNA during repair processes. A living organism's DNA needs constant maintenance. Every cell is in a state of fierce siege, as plentiful reactive oxygen compounds and ions constantly assault and damage the cell's organic molecules, especially its DNA. Oxidative damage to DNA is estimated to occur 10,000 times per day per cell. In order for life to survive this molecular battlefield, molecular countermeasures have evolved, among them a suite of complex molecules that detect oxidative damage to sections of DNA molecules, targeting those areas with various repair molecules that perform a series of elaborate molecular engineering operations necessary to fix the problem. The intimate mechanics of the complex molecular assemblies dedicated to the recognition, repair and signaling of DNA damage are still not fully understood. A specific protein structure known as the Zf-GRF domain is a mysterious component of APE2, a DNA-repair and DNA damage response enzyme, and is also common to a number of other DNA-maintaining molecules. A new research finding shows that Zf-GRF performs a critical DNA binding function in helping enzymes properly align to single-stranded DNA. The new study appears in a paper published online in PNAS on December 27, 2016. The article is titled "APE2 Zf-GRF Facilitates 3'-5' Resection of DNA Damage Following Oxidative Stress.” The finding is a result of two teams, one headed by Shan Yan from the Department of Biological Sciences at the University of North Carolina at Charlotte and the second headed by R.
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