%0 Journal Article %1 Elbatsh_2019 %A Elbatsh, Ahmed M.O. %A Kim, Eugene %A Eeftens, Jorine M. %A Raaijmakers, Jonne A. %A van der Weide, Robin H. %A Garc\'ıa-Nieto, Alberto %A Bravo, Sol %A Ganji, Mahipal %A uit de Bos, Jelmi %A Teunissen, Hans %A Medema, René H. %A de Wit, Elzo %A Haering, Christian H. %A Dekker, Cees %A Rowland, Benjamin D. %D 2019 %I Elsevier BV %J Molecular Cell %K haering %N 5 %P 724--737.e5 %R 10.1016/j.molcel.2019.09.020 %T Distinct Roles for Condensin's Two ATPase Sites in Chromosome Condensation %U https://doi.org/10.1016%2Fj.molcel.2019.09.020 %V 76 %X 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.

@article{Elbatsh_2019, 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.}, added-at = {2020-07-09T20:41:33.000+0200}, author = {Elbatsh, Ahmed M.O. and Kim, Eugene and Eeftens, Jorine M. and Raaijmakers, Jonne A. and van der Weide, Robin H. and Garc{\'{\i}}a-Nieto, Alberto and Bravo, Sol and Ganji, Mahipal and uit de Bos, Jelmi and Teunissen, Hans and Medema, Ren{\'{e}} H. and de Wit, Elzo and Haering, Christian H. and Dekker, Cees and Rowland, Benjamin D.}, biburl = {https://www.bibsonomy.org/bibtex/27da6e1e09d347bb711340983ed0cc7f8/bcz-wue}, doi = {10.1016/j.molcel.2019.09.020}, interhash = {8d144ca04553a9ace46f6a18873b1a82}, intrahash = {7da6e1e09d347bb711340983ed0cc7f8}, journal = {Molecular Cell}, keywords = {haering}, month = dec, number = 5, pages = {724--737.e5}, publisher = {Elsevier {BV}}, timestamp = {2024-07-31T17:37:30.000+0200}, title = {Distinct Roles for Condensin's Two {ATPase} Sites in Chromosome Condensation}, url = {https://doi.org/10.1016%2Fj.molcel.2019.09.020}, volume = 76, year = 2019 }