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.
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.”