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Journal Article

Distinct Roles for Condensin's Two ATPase Sites in Chromosome Condensation

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Ganji,  Mahipal
Jungmann, Ralf / Molecular Imaging and Bionanotechnology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Elbatsh, A. M. O., Kim, E., Eeftens, J. M., Raaijmakers, J. A., van der Weide, R. H., Garcia-Nieto, A., et al. (2019). Distinct Roles for Condensin's Two ATPase Sites in Chromosome Condensation. MOLECULAR CELL, 76(5), 724-737.e5. doi:10.1016/j.molcel.2019.09.020.


Cite as: http://hdl.handle.net/21.11116/0000-0005-73DE-0
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.