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

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, respect...

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Veröffentlicht in:	Nature structural & molecular biology Jg. 27; H. 8; S. 743 - 751
Hauptverfasser:	Lee, Byung-Gil, Merkel, Fabian, Allegretti, Matteo, Hassler, Markus, Cawood, Christopher, Lecomte, Léa, O'Reilly, Francis J, Sinn, Ludwig R, Gutierrez-Escribano, Pilar, Kschonsak, Marc, Bravo, Sol, Nakane, Takanori, Rappsilber, Juri, Aragon, Luis, Beck, Martin, Löwe, Jan, Haering, Christian H
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States Nature Publishing Group 01.08.2020
Schlagworte:	Adenosine triphosphatase Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphatases - ultrastructure Adenosine triphosphate Adenosine Triphosphate - metabolism Binding sites Carrier Proteins - chemistry Carrier Proteins - metabolism Carrier Proteins - ultrastructure Cell Cycle Proteins Chromosomal Proteins, Non-Histone - chemistry Chromosomal Proteins, Non-Histone - metabolism Chromosomal Proteins, Non-Histone - ultrastructure Chromosomes Cohesin Coils Condensin Conformation Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism DNA-Binding Proteins - ultrastructure Domains Extrusion Genomes Heat exchange Models, Molecular Molecular modelling Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Multiprotein Complexes - ultrastructure Nuclear Proteins - chemistry Nuclear Proteins - metabolism Nuclear Proteins - ultrastructure Nucleotides Open architectures Protein Conformation Protein Folding Protein Multimerization Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Translocation Yeast
ISSN:	1545-9993, 1545-9985, 1545-9985
Online-Zugang:	Volltext
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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.
Bibliographie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	1545-9993 1545-9985 1545-9985
DOI:	10.1038/s41594-020-0457-x