A folded conformation of MukBEF and cohesin

DOI: 10.1038/s41594-019-0196-z

Authors: Frank Bürmann (MRC Laboratory of Molecular Biology) , Byung-gil Lee (MRC Laboratory of Molecular Biology) , Thane Than (University of Sheffield) , Ludwig Sinn (Technische Universität Berlin) , Francis J. O'reilly (Technische Universität Berlin) , Stanislau Yatskevich (University of Oxford) , Juri Rappsilber (Technische Universität Berlin; Wellcome Centre for Cell Biology, University of Edinburgh) , Bin Hu (University of Sheffield) , Kim Nasmyth (University of Oxford) , Jan Lowe (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology , VOL 26 , PAGES 227 - 236

State: Published (Approved)
Published: March 2019
Diamond Proposal Number(s): 15916

Abstract: Structural maintenance of chromosomes (SMC)–kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA repair and regulation of gene expression. They function through the entrapment and active translocation of DNA, but the underlying conformational changes are largely unclear. Using structural biology, mass spectrometry and cross-linking, we investigated the architecture of two evolutionarily distant SMC–kleisin complexes: MukBEF from Escherichia coli, and cohesin from Saccharomyces cerevisiae. We show that both contain a dynamic coiled-coil discontinuity, the elbow, near the middle of their arms that permits a folded conformation. Bending at the elbow brings into proximity the hinge dimerization domain and the head–kleisin module, situated at opposite ends of the arms. Our findings favour SMC activity models that include a large conformational change in the arms, such as a relative movement between DNA contact sites during DNA loading and translocation.

Journal Keywords: Chromosomes; Structural biology

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

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