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  Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism

Lee, B.-G., Merkel, F., Allegretti, M., Hassler, M., Cawood, C., Lecomte, L., et al. (2020). Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism. Nature Structural and Molecular Biology, 27(8), 743-751. doi:10.1038/s41594-020-0457-x.

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Lee, Byung-Gil1, Author
Merkel, Fabian2, 3, Author
Allegretti, Matteo4, Author
Hassler, Markus2, 5, Author
Cawood, Christopher6, Author
Lecomte, Léa2, 3, Author
O'Reilly, Francis J.7, Author
Sinn, Ludwig R.7, Author
Gutierrez-Escribano, Pilar6, Author
Kschonsak, Marc2, Author
Bravo, Sol2, Author
Nakane, Takanori1, Author
Rappsilber, Juri7, 8, Author
Aragon, Luis6, Author
Beck, Martin2, 4, 9, Author              
Löwe, Jan1, Author
Haering, Christian H.2, 4, 5, Author
Affiliations:
1MRC Laboratory of Molecular Biology, Cambridge, UK, ou_persistent22              
2Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, ou_persistent22              
3Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences, Heidelberg, Germany, ou_persistent22              
4Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, ou_persistent22              
5Biocenter, Julius-Maximilians-Universität Würzburg, Würzburg, Germany, ou_persistent22              
6MRC London Institute of Medical Sciences, London, UK, ou_persistent22              
7Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany, ou_persistent22              
8Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK, ou_persistent22              
9Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society, ou_3040395              

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 Abstract: Complexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought to fold interphase and mitotic chromosomes, respectively, into large loop domains, although the underlying molecular mechanisms have remained unknown. We used cryo-EM to investigate the nucleotide-driven reaction cycle of condensin from the budding yeast Saccharomyces cerevisiae. Our structures of the five-subunit condensin holo complex at different functional stages suggest that ATP binding induces the transition of the SMC coiled coils from a folded-rod conformation into a more open architecture. ATP binding simultaneously triggers the exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains. We propose that these steps result in the interconversion of DNA-binding sites in the catalytic core of condensin, forming the basis of the DNA translocation and loop-extrusion activities.

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Language(s): eng - English
 Dates: 2020-03-252020-05-282020-07-132020-08
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41594-020-0457-x
BibTex Citekey: lee_cryo-em_2020
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Title: Nature Structural and Molecular Biology
  Other : Nature Struct Biol
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 27 (8) Sequence Number: - Start / End Page: 743 - 751 Identifier: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763