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Structural Basis of an Asymmetric Condensin ATPase Cycle

Title data

Hassler, Markus ; Shaltiel, Indra A. ; Kschonsak, Marc ; Simon, Bernd ; Merkel, Fabian ; Thärichen, Lena ; Bailey, Henry J. ; Macošek, Jakub ; Bravo, Sol ; Metz, Jutta ; Hennig, Janosch ; Haering, Christian H.:
Structural Basis of an Asymmetric Condensin ATPase Cycle.
In: Molecular Cell. Vol. 74 (2019) Issue 6 . - S. 1175-1188.e9.
ISSN 1097-4164
DOI: https://doi.org/10.1016/j.molcel.2019.03.037

Abstract in another language

The condensin protein complex plays a key role in the structural organization of genomes. How the ATPase activity of its SMC subunits drives large-scale changes in chromosome topology has remained unknown. Here we reconstruct, at near-atomic resolution, the sequence of events that take place during the condensin ATPase cycle. We show that ATP binding induces a conformational switch in the Smc4 head domain that releases its hitherto undescribed interaction with the Ycs4 HEAT-repeat subunit and promotes its engagement with the Smc2 head into an asymmetric heterodimer. SMC head dimerization subsequently enables nucleotide binding at the second active site and disengages the Brn1 kleisin subunit from the Smc2 coiled coil to open the condensin ring. These large-scale transitions in the condensin architecture lay out a mechanistic path for its ability to extrude DNA helices into large loop structures.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: condensin; cohesin; SMC protein complex; ABC ATPase; DNA loop extrusion; mitotic chromosome; genome organization; structural biology
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 06 Oct 2021 11:18
Last Modified: 06 Oct 2021 11:18
URI: https://eref.uni-bayreuth.de/id/eprint/67210