DNA binding to SMC ATPases—trapped for release

The SMC/Rad50/RecN proteins are universal DNA‐associated ABC‐type ATPases with crucial functions in genome maintenance. New insights into Rad50–DNA complex structure and cohesin regulation inspire a speculative look at the entire superfamily. Identification of a continuous DNA binding site across the Rad50 dimer interface (Liu et al , [2015][1]; Seifert et al , [2016][2]) suggests a similar site in cohesin. The localization of this site hints a DNA‐activated mechanism for cohesin removal from chromosomes. [1]: #ref-8 [2]: #ref-10