Topology and structure of an engineered human cohesin complex bound to Pds5B

Michael T. Hons, Pim J. Huis in ‘t Veld (), Jan Kaesler, Pascaline Rombaut, Alexander Schleiffer, Franz Herzog, Holger Stark () and Jan-Michael Peters ()
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Michael T. Hons: Max Planck Institute for Biophysical Chemistry
Pim J. Huis in ‘t Veld: Research Institute of Molecular Pathology (IMP)
Jan Kaesler: Max Planck Institute for Biophysical Chemistry
Pascaline Rombaut: Gene Center, Ludwig-Maximilian University
Alexander Schleiffer: Research Institute of Molecular Pathology (IMP)
Franz Herzog: Gene Center, Ludwig-Maximilian University
Holger Stark: Max Planck Institute for Biophysical Chemistry
Jan-Michael Peters: Research Institute of Molecular Pathology (IMP)

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract The cohesin subunits Smc1, Smc3 and Scc1 form large tripartite rings which mediate sister chromatid cohesion and chromatin structure. These are thought to entrap DNA with the help of the associated proteins SA1/2 and Pds5A/B. Structural information is available for parts of cohesin, but analyses of entire cohesin complexes are limited by their flexibility. Here we generated a more rigid ‘bonsai’ cohesin by truncating the coiled coils of Smc1 and Smc3 and used single-particle electron microscopy, chemical crosslinking-mass spectrometry and in silico modelling to generate three-dimensional models of cohesin bound to Pds5B. The HEAT-repeat protein Pds5B forms a curved structure around the nucleotide-binding domains of Smc1 and Smc3 and bridges the Smc3-Scc1 and SA1-Scc1 interfaces. These results indicate that Pds5B forms an integral part of the cohesin ring by contacting all other cohesin subunits, a property that may reflect the complex role of Pds5 proteins in controlling cohesin–DNA interactions.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12523

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DOI: 10.1038/ncomms12523

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