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Biochemical reconstitution of topological DNA binding by the cohesin ring

Author

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  • Yasuto Murayama

    (Chromosome Segregation Laboratory, Cancer Research UK London Research Institute, 44 Lincoln’s Inn Fields, London WC2A 3LY, UK)

  • Frank Uhlmann

    (Chromosome Segregation Laboratory, Cancer Research UK London Research Institute, 44 Lincoln’s Inn Fields, London WC2A 3LY, UK)

Abstract

Cohesion between sister chromatids, mediated by the chromosomal cohesin complex, is a prerequisite for faithful chromosome segregation in mitosis. Cohesin also has vital roles in DNA repair and transcriptional regulation. The ring-shaped cohesin complex is thought to encircle sister DNA strands, but its molecular mechanism of action is poorly understood and the biochemical reconstitution of cohesin activity in vitro has remained an unattained goal. Here we reconstitute cohesin loading onto DNA using purified fission yeast cohesin and its loader complex, Mis4Scc2–Ssl3Scc4 (Schizosaccharomyces pombe gene names appear throughout with their more commonly known Saccharomyces cerevisiae counterparts added in superscript). Incubation of cohesin with DNA leads to spontaneous topological loading, but this remains inefficient. The loader contacts cohesin at multiple sites around the ring circumference, including the hitherto enigmatic Psc3Scc3 subunit, and stimulates cohesin’s ATPase, resulting in efficient topological loading. The in vitro reconstitution of cohesin loading onto DNA provides mechanistic insight into the initial steps of the establishment of sister chromatid cohesion and other chromosomal processes mediated by cohesin.

Suggested Citation

  • Yasuto Murayama & Frank Uhlmann, 2014. "Biochemical reconstitution of topological DNA binding by the cohesin ring," Nature, Nature, vol. 505(7483), pages 367-371, January.
    • Handle: RePEc:nat:nature:v:505:y:2014:i:7483:d:10.1038_nature12867
    DOI: 10.1038/nature12867
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    Cited by:

    1. Aditi Kaushik & Thane Than & Naomi J. Petela & Menelaos Voulgaris & Charlotte Percival & Peter Daniels & John B. Rafferty & Kim A. Nasmyth & Bin Hu, 2023. "Conformational dynamics of cohesin/Scc2 loading complex are regulated by Smc3 acetylation and ATP binding," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Ignacio Prusén Mota & Marta Galova & Alexander Schleiffer & Tan-Trung Nguyen & Ines Kovacikova & Carolina Farias Saad & Gabriele Litos & Tomoko Nishiyama & Juraj Gregan & Jan-Michael Peters & Peter Sc, 2024. "Sororin is an evolutionary conserved antagonist of WAPL," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    3. Dácil Alonso-Gil & Ana Cuadrado & Daniel Giménez-Llorente & Miriam Rodríguez-Corsino & Ana Losada, 2023. "Different NIPBL requirements of cohesin-STAG1 and cohesin-STAG2," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    4. 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.
    5. Sofía Muñoz & Andrew Jones & Céline Bouchoux & Tegan Gilmore & Harshil Patel & Frank Uhlmann, 2022. "Functional crosstalk between the cohesin loader and chromatin remodelers," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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