title: DNA binding to SMC ATPases-trapped for release.
abstract: 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, 2016; Seifert et al, 2016) suggests a similar site in cohesin. The localization of this site hints a DNA-activated mechanism for cohesin removal from chromosomes.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
authors.forename: Herwig
authors.initials: H
authors.lastname: Schüler
authors.affiliation: Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
authors.forename: Camilla
authors.initials: C
authors.lastname: Sjögren
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism*; D002597:Chaetomium / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004271:DNA, Fungal / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D017017:Methanococcus / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D004271:DNA, Fungal; D005656:Fungal Proteins; D000255:Adenosine Triphosphate; D004247:DNA