Rockefeller University researchers
found that part of a DNA repair protein known as 53BP1 fits over the phosphorylated part of H2AX “like a glove,” says Kleiner. This interaction helps bring 53BP1 to the site of DNA damage, where it mediates the repair of double-stranded breaks in DNA by encouraging the repair machinery to glue the two ends back together.
New findings shed light on fundamental process of DNA repair
What are the prospects of a DNA self replicating entity surviving with rapid cumulative DNA mutations until it assembles the DNA repair mechanism – by random stochastic processes?
Paper: Chemical proteomics reveals a γH2AX-53BP1 interaction in the DNA damage response Ralph E Kleiner et al. Nature Chemical Biology (2015) 07 September 2015 doi:10.1038/nchembio.1908
For context, see John C. Sanford’s “Genetic Entropy and the Mystery of the Genome.”
For such insightful details elegantly explained, see Dr. Howard Glicksman’s Exercise Your Wonder: Beyond Irreducible Complexity. e.g.,
CAUTION: ENZYMES AT WORK: Part III: Anti-Clotting