Distinct Roles for Condensin's Two ATPase Sites in Chromosome Condensation
Ahmed M.O. Elbatsh (Nederlands Kanker Instituut - Antoni van Leeuwenhoek ziekenhuis)
Eugene Kim (BN/Cees Dekker Lab, Kavli institute of nanoscience Delft)
Jorine M. Eeftens (BN/Cees Dekker Lab, Kavli institute of nanoscience Delft)
Jonne A. Raaijmakers (Nederlands Kanker Instituut - Antoni van Leeuwenhoek ziekenhuis)
Robin H. van der Weide (Nederlands Kanker Instituut - Antoni van Leeuwenhoek ziekenhuis)
Alberto García-Nieto (Nederlands Kanker Instituut - Antoni van Leeuwenhoek ziekenhuis)
Sol Bravo (European Molecular Biology Laboratory)
Mahipal Ganji (Kavli institute of nanoscience Delft, BN/Cees Dekker Lab)
Cees Dekker (Kavli institute of nanoscience Delft, BN/Cees Dekker Lab)
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Abstract
Condensin is a conserved SMC complex that uses its ATPase machinery to structure genomes, but how it does so is largely unknown. We show that condensin's ATPase has a dual role in chromosome condensation. Mutation of one ATPase site impairs condensation, while mutating the second site results in hyperactive condensin that compacts DNA faster than wild-type, both in vivo and in vitro. Whereas one site drives loop formation, the second site is involved in the formation of more stable higher-order Z loop structures. Using hyperactive condensin I, we reveal that condensin II is not intrinsically needed for the shortening of mitotic chromosomes. Condensin II rather is required for a straight chromosomal axis and enables faithful chromosome segregation by counteracting the formation of ultrafine DNA bridges. SMC complexes with distinct roles for each ATPase site likely reflect a universal principle that enables these molecular machines to intricately control chromosome architecture.
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