Soh, Young-Min, Bürmann, Frank, Shin, Ho-Chul, Oda, Takashi, Jin, Kyeong Sik, Toseland, Christopher P., Kim, Cheolhee, Lee, Hansol, Kim, Soo Jin, Kong, Min-Seok, and others. (2015) Molecular basis for SMC rod formation and its dissolution upon DNA binding. Molecular cell, 57 (2). pp. 290-303. ISSN 1097-4164. (doi:10.1016/j.molcel.2014.11.023) (KAR id:47844)
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| Official URL http://dx.doi.org/10.1016/j.molcel.2014.11.023 |
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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.
| Item Type: | Article |
|---|---|
| DOI/Identification number: | 10.1016/j.molcel.2014.11.023 |
| Subjects: | Q Science |
| Divisions: | Divisions > Division of Natural Sciences > School of Biosciences |
| Depositing User: | Chris Toseland |
| Date Deposited: | 07 Apr 2015 12:01 UTC |
| Last Modified: | 29 May 2019 14:23 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/47844 (The current URI for this page, for reference purposes) |
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