Molecular Basis for SMC Rod Formation and Its Dissolution upon DNA Binding

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SMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive "hinge'' dimerization domain with an ATP-regulated "head'' dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB's association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc's dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome.
Publisher
CELL PRESS
Issue Date
2015-01
Language
English
Article Type
Article
Keywords

X-RAY-SCATTERING; HINGE DOMAIN; CHROMOSOME CONDENSATION; FUNCTIONAL IMPLICATIONS; STRUCTURAL MAINTENANCE; BACILLUS-SUBTILIS; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; ATP HYDROLYSIS; COMPLEX

Citation

MOLECULAR CELL, v.57, no.2, pp.290 - 303

ISSN
1097-2765
DOI
10.1016/j.molcel.2014.11.023
URI
http://hdl.handle.net/10203/195458
Appears in Collection
MSE-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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