Bret Freudenthal @freudlab.bsky.social · 11/08/20264/ MD simulations from the Bignon lab agree: the same two-state conformational exchange and the same local backbone perturbations in nucleosomal and non-nucleosomal DNA. 100
Bret Freudenthal @freudlab.bsky.social · 11/08/20265/ MUTYH needs to engage both strands with its N- and C-terminal domains. Modeling shows it cannot do that in an NCP without clashing into the histones. Steric exclusion, not altered lesion presentation, is the barrier. 100
Bret Freudenthal @freudlab.bsky.social · 11/08/20266/ This fits MUTYH as a post-replicative enzyme working at the fork, and gives a mechanistic explanation for elevated G to T transversions in histone-bound DNA after oxidative stress. 100
