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Instruments / Technical Area	Publication Details	Published
Krios I-Titan Krios I at Diamond	Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism Byung-gil Lee , Fabian Merkel , Matteo Allegretti , Markus Hassler , Christopher Cawood , Léa Lecomte , Francis J. O'reilly , Ludwig R. Sinn , Pilar Gutierrez-escribano , Marc Kschonsak , Sol Bravo , Takanori Nakane , Juri Rappsilber , Luis Aragon , Martin Beck , Jan Lowe , Christian H. Haering Nature Structural & Molecular Biology 53 DOI: 10.1038/s41594-020-0457-x Show Abstract ▼ Abstract: Complexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought to fold interphase and mitotic chromosomes, respectively, into large loop domains, although the underlying molecular mechanisms have remained unknown. We used cryo-EM to investigate the nucleotide-driven reaction cycle of condensin from the budding yeast Saccharomyces cerevisiae. Our structures of the five-subunit condensin holo complex at different functional stages suggest that ATP binding induces the transition of the SMC coiled coils from a folded-rod conformation into a more open architecture. ATP binding simultaneously triggers the exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains. We propose that these steps result in the interconversion of DNA-binding sites in the catalytic core of condensin, forming the basis of the DNA translocation and loop-extrusion activities.	Jul 2020
I04-1-Macromolecular Crystallography (fixed wavelength)	A folded conformation of MukBEF and cohesin Frank Bürmann , Byung-gil Lee , Thane Than , Ludwig Sinn , Francis J. O'reilly , Stanislau Yatskevich , Juri Rappsilber , Bin Hu , Kim Nasmyth , Jan Lowe Nature Structural & Molecular Biology 26, 227 - 236 DOI: 10.1038/s41594-019-0196-z Diamond Proposal Number(s): [15916] Show Abstract ▼ 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.	Mar 2019
I03-Macromolecular Crystallography	Crystal Structure of the Cohesin Gatekeeper Pds5 and in Complex with Kleisin Scc1 Byung-gil Lee , Maurici b. Roig , Marijke Jansma , Naomi Petela , Jean Metson , Kim Nasmyth , Jan Löwe Cell Reports 14 (9), 2108–2115 DOI: 10.1016/j.celrep.2016.02.020 Open Access Show Abstract ▼ Abstract: Sister chromatid cohesion is mediated by cohesin, whose Smc1, Smc3, and kleisin (Scc1) subunits form a ring structure that entraps sister DNAs. The ring is opened either by separase, which cleaves Scc1 during anaphase, or by a releasing activity involving Wapl, Scc3, and Pds5, which bind to Scc1 and open its interface with Smc3. We present crystal structures of Pds5 from the yeast L. thermotolerans in the presence and absence of the conserved Scc1 region that interacts with Pds5. Scc1 binds along the spine of the Pds5 HEAT repeat fold and is wedged between the spine and C-terminal hook of Pds5. We have isolated mutants that confirm the observed binding mode of Scc1 and verified their effect on cohesin by immunoprecipitation and calibrated ChIP-seq. The Pds5 structure also reveals architectural similarities to Scc3, the other large HEAT repeat protein of cohesin and, most likely, Scc2.	Mar 2016

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