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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, Autor
Merkel, Fabian2, 3, Autor
Allegretti, Matteo4, Autor
Hassler, Markus2, 5, Autor
Cawood, Christopher6, Autor
Lecomte, Léa2, 3, Autor
O'Reilly, Francis J.7, Autor
Sinn, Ludwig R.7, Autor
Gutierrez-Escribano, Pilar6, Autor
Kschonsak, Marc2, Autor
Bravo, Sol2, Autor
Nakane, Takanori1, Autor
Rappsilber, Juri7, 8, Autor
Aragon, Luis6, Autor
Beck, Martin2, 4, 9, Autor           
Löwe, Jan1, Autor
Haering, Christian H.2, 4, 5, Autor
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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 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2020-03-252020-05-282020-07-132020-08
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1038/s41594-020-0457-x
BibTex Citekey: lee_cryo-em_2020
 Art des Abschluß: -

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Titel: Nature Structural and Molecular Biology
  Andere : Nature Struct Biol
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: New York, NY : Nature Pub. Group
Seiten: - Band / Heft: 27 (8) Artikelnummer: - Start- / Endseite: 743 - 751 Identifikator: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763