Nature structural & molecular biology, 2020-08, Vol.27 (8), p.743-751
2020
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Cryo-EM structures of holo condensin reveal a subunit flip-flop mechanism
- Ist Teil von
- Nature structural & molecular biology, 2020-08, Vol.27 (8), p.743-751
- Ort / Verlag
- United States
- Erscheinungsjahr
- 2020
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1545-9993eISSN: 1545-9985DOI: 10.1038/s41594-020-0457-xTitel-ID: cdi_pubmed_primary_32661420
- Format
- –
- Schlagworte
- Adenosine Triphosphatases - chemistry, Adenosine Triphosphatases - metabolism, Adenosine Triphosphatases - ultrastructure, Adenosine Triphosphate - metabolism, 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, Cryoelectron Microscopy, DNA-Binding Proteins - chemistry, DNA-Binding Proteins - metabolism, DNA-Binding Proteins - ultrastructure, Models, Molecular, Multiprotein Complexes - chemistry, Multiprotein Complexes - metabolism, Multiprotein Complexes - ultrastructure, Nuclear Proteins - chemistry, Nuclear Proteins - metabolism, Nuclear Proteins - ultrastructure, Protein Conformation, Protein Folding, Protein Multimerization, Saccharomyces cerevisiae - chemistry, Saccharomyces cerevisiae - metabolism, Saccharomyces cerevisiae Proteins - chemistry, Saccharomyces cerevisiae Proteins - metabolism, Saccharomyces cerevisiae Proteins - ultrastructure