Marc Kschonsak

TL;DR: A direct DNA-binding site is identified in the eukaryotic condensin complex, which is formed by its Ycg 1Cnd3 HEAT-repeat and Brn1Cnd2 kleisin subunits, and the data suggest a sophisticated molecular basis for anchoring condensIn complexes to chromosomes that enables the formation of large-sized chromatin loops.

TL;DR: It is shown that the Smc2-Smc4 coiled coils are highly flexible polymers with a persistence length of only ∼4 nm, and it is demonstrated that the SMC dimers can adopt various architectures that interconvert dynamically over time.

TL;DR: A stepwise model of mitotic chromosome condensation is proposed that envisions the sequential generation of intra- Chromosomal linkages by condensin complexes in the context of cohesin-mediated inter-chromosomal linksages, assisted by topoisomerase II.

TL;DR: Cryo-EM structures of the S. cerevisiae condensin holo complex reveal that ATP binding triggers exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains, potentially leading to an interconversion of DNA-binding sites in the catalytic core ofcondensin that might form the basis of its DNA translocation and loop-extrusion activities.

TL;DR: This work employs single‐molecule magnetic tweezers to measure, in real time, the compaction of individual DNA molecules by the budding yeast condensin complex, and indicates that compaction can proceed in large steps, driving DNA molecules into a fully condensed state against forces of up to 2 pN.