Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The structure of the dimeric replication initiator of pPS10 reveals that secondary structure remodeling of chameleon sequences defines the monomer-dimer oligomerization state of the protein. Together with an unanticipated dimerization interface, this result will steer thinking in the field and influence strategies to control spread of virulence and antibiotic resistance genes that are often plasmid-encoded.
The structure of the CH1 domain of p300 in complex with the transactivation domain of CITED2 brings us one step closer toward understanding the molecular basis of the regulation of hypoxia response.
Two recent papers provide evidence that the Escherichia coli RecBCD complex, which unwinds double-stranded DNA to supply a substrate for recombination, has two helicase subunits that bind opposite DNA strands and move with opposite unwinding 'polarities'.