Molecular basis for SMC rod formation and its dissolution upon DNA binding
SCIE
SCOPUS
- Title
- Molecular basis for SMC rod formation and its dissolution upon DNA binding
- Authors
- Soh, YM; Burmann, F; Shin, HC; Oda, T; Jin, KS; C. P. Toseland; C. Kim; Kim, C; S. J. Kim; M-S Kong; M-L Durand-Diebold; Y.-G. Kim; -Diebold, ML; Kim, YG; Kim, HM; Lee, NK; S. Gruber; Oh, BH; Gruber, S
- Date Issued
- 2015-01-22
- Publisher
- Cell Press
- Abstract
- 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/13580
- DOI
- 10.1016/J.MOLCEL.2014.11.023
- ISSN
- 1097-2765
- Article Type
- Article
- Citation
- Molecular Cell, vol. 57, no. 2, page. 290 - 303, 2015-01-22
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