Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms14011
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Funding
- Cancer Research UK Programme Grant [C302/A14532]
- MRC [G1001668, G0901011, G1100074]
- MRC [G1001668, G0901011, G1100074] Funding Source: UKRI
- Cancer Research UK [14532, 24386] Funding Source: researchfish
- Medical Research Council [G1001668, G0901011, G1100074] Funding Source: researchfish
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The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is scaffolded by a specific SMC protein dimer (heterodimer in eukaryotes) held together via their hinge domains. Here we show that the Smc5/6-hinge, like those of cohesin and condensin, also forms a toroidal structure but with distinctive subunit interfaces absent from the other SMC complexes; an unusual 'molecular latch' and a functional 'hub'. Defined mutations in these interfaces cause severe phenotypic effects with sensitivity to DNA-damaging agents in fission yeast and reduced viability in human cells. We show that the Smc5/6-hinge complex binds preferentially to ssDNA and that this interaction is affected by both ` latch' and ` hub' mutations, suggesting a key role for these unique features in controlling DNA association by the Smc5/6 complex.
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