Upon genotoxic stress, the FBXL10-RNF68-RNF2 ubiquitin ligase complex mono-ubiquitylates histone H2A and mediates H2A/H2A.Z exchange to repress transcription and ensures proper high fidelity homologous recombination repair.
A structural model of the dynamic complex comprising the histone reader RNF169 bound to an ubiquitylated nucleosome core particle reveals a three-pronged binding mechanism, which provides specificity for the recognition of DNA double-strand break sites.
Publication bias, in which positive results are preferentially reported by authors and published by journals, can restrict the visibility of evidence against false claims and allow such claims to be canonized inappropriately as facts.
Neuronal participation in generation of motor patterns in the spinal circuits is lognormal, which is an indication of a rich diversity of activity within the mean-driven as well as the fluctuation-driven regimes.
Integration of structural bioinformatics and free-energy simulations reveals how a helicase switches its function from unwinding to rezipping DNA, during which a key metastable conformation is predicted and verified by single-molecule measurements.