A novel synthetic DNA cassette of CTCF-binding sites combined with the drug-controllable induction system of heterochromatin enabled switchable blocking of chromatin conformation and gene-enhancer interaction.
The structure of the recombination complex responsible for flagellar antigen switching in Salmonella enterica, and the mechanism that regulates the site-specific DNA inversion reaction, have been determined.
The Cohesin subunit Scc3 contains a hook-shaped domain that binds to DNA substrate, thus revealing that Cohesin-chromatin transactions are driven not only by topological interactions, but also by direct protein-DNA contacts.
Absolute quantification of CTCF and cohesin reveals quantitative constraints on 3D genome organization and illuminates the molecular architecture of the cohesin complex.
A statistical model rescues multi-mapping reads with high accuracy and demonstrates their impact in all facets of the analysis of genome-wide high throughput conformation capture datasets.
Autonomous patterns of cell contraction in the context of localized apical extracellular matrix constraints specify tissue stresses that reshape the wing epithelium.
Rigorous biochemical and structural analyses reveal the precise topology of cohesin's association with DNA and suggest a mechanism for how DNA is transported inside the ring.