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

Author

Listed:
  • Aaron Alt

    (Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Hung Q. Dang

    (Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Owen S. Wells

    (Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Luis M. Polo

    (Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Matt A. Smith

    (Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Grant A. McGregor

    (Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Thomas Welte

    (Dynamic Biosensors GmbH, Lochhamer Strasse)

  • Alan R. Lehmann

    (Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Laurence H. Pearl

    (Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Johanne M. Murray

    (Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

  • Antony W. Oliver

    (Cancer Research UK DNA Repair Enzymes Group, Genome Damage and Stability Centre, School of Life Sciences, University of Sussex)

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.

Suggested Citation

  • Aaron Alt & Hung Q. Dang & Owen S. Wells & Luis M. Polo & Matt A. Smith & Grant A. McGregor & Thomas Welte & Alan R. Lehmann & Laurence H. Pearl & Johanne M. Murray & Antony W. Oliver, 2017. "Specialized interfaces of Smc5/6 control hinge stability and DNA association," Nature Communications, Nature, vol. 8(1), pages 1-14, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14011
    DOI: 10.1038/ncomms14011
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    Cited by:

    1. Jeremy T-H. Chang & Shibai Li & Emily C. Beckwitt & Thane Than & Cory Haluska & Joshua Chandanani & Michael E. O’Donnell & Xiaolan Zhao & Shixin Liu, 2022. "Smc5/6’s multifaceted DNA binding capacities stabilize branched DNA structures," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Ryota Takaki & Atreya Dey & Guang Shi & D. Thirumalai, 2021. "Theory and simulations of condensin mediated loop extrusion in DNA," Nature Communications, Nature, vol. 12(1), pages 1-10, December.

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