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The cohesin ring concatenates sister DNA molecules

Author

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  • Christian H. Haering

    (University of Oxford, South Parks Road, Oxford OX1 3QU, UK
    Present addresses: European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany (C.H.H.); Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK (P.A.).)

  • Ana-Maria Farcas

    (University of Oxford, South Parks Road, Oxford OX1 3QU, UK)

  • Prakash Arumugam

    (University of Oxford, South Parks Road, Oxford OX1 3QU, UK
    Present addresses: European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany (C.H.H.); Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK (P.A.).)

  • Jean Metson

    (University of Oxford, South Parks Road, Oxford OX1 3QU, UK)

  • Kim Nasmyth

    (University of Oxford, South Parks Road, Oxford OX1 3QU, UK)

Abstract

Sister chromatid cohesion, which is essential for mitosis, is mediated by a multi-subunit protein complex called cohesin. Cohesin’s Scc1, Smc1 and Smc3 subunits form a tripartite ring structure, and it has been proposed that cohesin holds sister DNA molecules together by trapping them inside its ring. To test this, we used site-specific crosslinking to create chemical connections at the three interfaces between the three constituent polypeptides of the ring, thereby creating covalently closed cohesin rings. As predicted by the ring entrapment model, this procedure produced dimeric DNA–cohesin structures that are resistant to protein denaturation. We conclude that cohesin rings concatenate individual sister minichromosome DNA molecules.

Suggested Citation

  • Christian H. Haering & Ana-Maria Farcas & Prakash Arumugam & Jean Metson & Kim Nasmyth, 2008. "The cohesin ring concatenates sister DNA molecules," Nature, Nature, vol. 454(7202), pages 297-301, July.
    • Handle: RePEc:nat:nature:v:454:y:2008:i:7202:d:10.1038_nature07098
    DOI: 10.1038/nature07098
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    Cited by:

    1. Daniel Bsteh & Hagar F. Moussa & Georg Michlits & Ramesh Yelagandula & Jingkui Wang & Ulrich Elling & Oliver Bell, 2023. "Loss of cohesin regulator PDS5A reveals repressive role of Polycomb loops," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Georgii Pobegalov & Lee-Ya Chu & Jan-Michael Peters & Maxim I. Molodtsov, 2023. "Single cohesin molecules generate force by two distinct mechanisms," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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