All eukaryotic SMC proteins induce a twist of -0.6 at each DNA loop extrusion step
Richard Janissen (TU Delft - BN/Bionanoscience, Deggendorf Institute of Technology, Kavli institute of nanoscience Delft)
Roman Barth (Kavli institute of nanoscience Delft, TU Delft - BN/Cees Dekker Lab)
Iain F. Davidson (Research Institute of Molecular Pathology, Vienna)
Jan Michael Peters (Research Institute of Molecular Pathology, Vienna)
Cees Dekker (Kavli institute of nanoscience Delft, TU Delft - BN/Cees Dekker Lab)
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Abstract
Eukaryotes carry three types of structural maintenance of chromosome (SMC) protein complexes, condensin, cohesin, and SMC5/6, which are ATP-dependent motor proteins that remodel the genome via DNA loop extrusion (LE). SMCs modulate DNA supercoiling but remains incompletely understood how this is achieved. Using a single-molecule magnetic tweezers assay that directly measures how much twist is induced by individual SMCs in each LE step, we demonstrate that all three SMC complexes induce the same large negative twist (i.e., linking number change ΔL
k of ~−0.6 at each LE step) into the extruded loop, independent of step size and DNA tension. Using ATP hydrolysis mutants and nonhydrolyzable ATP analogs, we find that ATP binding is the twist-inducing event during the ATPase cycle, coinciding with the force-generating LE step. The fact that all three eukaryotic SMC proteins induce the same amount of twist indicates a common DNA-LE mechanism among these SMC complexes.
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