1. DNA binding to SMC ATPases—trapped for release
- Author
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Herwig Schüler and Camilla Sjögren
- Subjects
0301 basic medicine ,Genetics ,Fungal protein ,Methanococcus ,General Immunology and Microbiology ,Cohesin ,biology ,General Neuroscience ,ATPase ,biology.organism_classification ,General Biochemistry, Genetics and Molecular Biology ,Cell biology ,DNA binding site ,enzymes and coenzymes (carbohydrates) ,03 medical and health sciences ,chemistry.chemical_compound ,030104 developmental biology ,chemistry ,Rad50 ,biology.protein ,biological phenomena, cell phenomena, and immunity ,Molecular Biology ,Adenosine triphosphate ,DNA - 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.
- Published
- 2016
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