To protect the integrity of the genetic code, cells remove
8-oxoguanine from their DNA with a repair enzyme called OGG1.
OGG1 does its job by attaching to a damaged base, cutting it
free from the DNA molecule, and then releasing it. Boldogh and
his collaborators found that their key byproduct was being
produced just after this repair process was completed. Analyzing
test-tube, cell-culture and mouse experimental data, they
realized that immediately after being released by OGG1,
8-oxoguanine reunites with the repair enzyme, attaching at a
bonding site different from the one used previously. And the
resulting 8-oxoguanine-OGG1 complex, they found, has the ability
to activate the powerful Ras signaling pathways, some of the
most important biochemical networks in the cell. "Ras family
proteins are involved in almost every cell function: metabolism,
activation of genes, growth signals, inflammation signals,
apoptosis," Boldogh said. "Because it activates Ras pathways,
the release of 8-oxoguanine in DNA base repair