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DNA binding to SMC ATPases—trapped for release
- Source :
- The EMBO Journal. 35:703-705
- Publication Year :
- 2016
- Publisher :
- EMBO, 2016.
-
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.
- 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
Subjects
Details
- ISSN :
- 14602075 and 02614189
- Volume :
- 35
- Database :
- OpenAIRE
- Journal :
- The EMBO Journal
- Accession number :
- edsair.doi...........4ecf82e4a293b6be47dace0edf0ab373