Conformational dynamics of cohesin/Scc2 loading complex are regulated by Smc3 acetylation and ATP binding

Aditi Kaushik, Thane Than, Naomi J. Petela, Menelaos Voulgaris, Charlotte Percival, Peter Daniels, John B. Rafferty, Kim A. Nasmyth and Bin Hu ()
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Aditi Kaushik: University of Aberdeen
Thane Than: University of Sheffield
Naomi J. Petela: University of Oxford
Menelaos Voulgaris: University of Oxford
Charlotte Percival: University of Sheffield
Peter Daniels: University of Sheffield
John B. Rafferty: University of Sheffield
Kim A. Nasmyth: University of Oxford
Bin Hu: University of Aberdeen

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: Abstract The ring-shaped cohesin complex is a key player in sister chromatid cohesion, DNA repair, and gene transcription. The loading of cohesin to chromosomes requires the loader Scc2 and is regulated by ATP. This process is hindered by Smc3 acetylation. However, the molecular mechanism underlying this inhibition remains mysterious. Here, using Saccharomyces cerevisiae as a model system, we identify a novel configuration of Scc2 with pre-engaged cohesin and reveal dynamic conformations of the cohesin/Scc2 complex in the loading reaction. We demonstrate that Smc3 acetylation blocks the association of Scc2 with pre-engaged cohesin by impairing the interaction of Scc2 with Smc3’s head. Lastly, we show that ATP binding induces the cohesin/Scc2 complex to clamp DNA by promoting the interaction between Scc2 and Smc3 coiled coil. Our results illuminate a dynamic reconfiguration of the cohesin/Scc2 complex during loading and indicate how Smc3 acetylation and ATP regulate this process.

Date: 2023
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DOI: 10.1038/s41467-023-41596-w

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