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Specialized interfaces of Smc5/6 control hinge stability and DNA association

DOI: 10.1038/ncomms14011 DOI Help

Authors: Aaron Alt (University of Sussex) , Hung Q. Dang (University of Sussex) , Owen S. Wells (University of Sussex) , Luis M. Polo (University of Sussex) , Matt A. Smith (University of Sussex) , Grant A. Mcgregor (University of Sussex) , Thomas Welte (Dynamic Biosensors GmbH) , Alan R. Lehmann (University of Sussex) , Laurence H. Pearl (University of Sussex) , Johanne M. Murray (University of Sussex) , Antony W. Oliver (University of Sussex)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: January 2017
Diamond Proposal Number(s): 10088 , 6385

Open Access Open Access

Abstract: 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.

Journal Keywords: Chromosome segregation; Chromosomes; DNA-binding proteins; Structural biology

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: B21-High Throughput SAXS , I04-Macromolecular Crystallography

Added On: 06/02/2017 10:25

Documents:
ncomms14011.pdf

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