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TitleCryo-EM structures of holo condensin reveal a subunit flip-flop mechanism.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 8, Page 743-751, Year 2020
Publish dateJul 13, 2020
AuthorsByung-Gil Lee / Fabian Merkel / Matteo Allegretti / Markus Hassler / Christopher Cawood / Léa Lecomte / Francis J O'Reilly / Ludwig R Sinn / Pilar Gutierrez-Escribano / Marc Kschonsak / Sol Bravo / Takanori Nakane / Juri Rappsilber / Luis Aragon / Martin Beck / Jan Löwe / Christian H Haering /
PubMed AbstractComplexes 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 ...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.
External linksNat Struct Mol Biol / PubMed:32661420 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 9.1 Å
Structure data

10944

6yvd

EMDB-10944, PDB-6yvd:
Head segment of the S.cerevisiae condensin holocomplex in presence of ATP
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-10947:
Condensin complex from S.cerevisiae ATP-free apo non-engaged state: focused refinement on arm segment
Method: EM (single particle) / Resolution: 5.3 Å

EMDB-10948:
Condensin complex from S.cerevisiae ATP-free apo non-engaged state: focused refinement on head segment
Method: EM (single particle) / Resolution: 4.2 Å

10951

6yvu

EMDB-10951: Condensin complex from S.cerevisiae ATP-free apo non-engaged state: overall map
PDB-6yvu: Condensin complex from S.cerevisiae ATP-free apo non-engaged state
Method: EM (single particle) / Resolution: 7.5 Å

10952

6yvv

EMDB-10952: Condensin complex from S.cerevisiae ATP-free apo bridged state: focused refinement on head segment
PDB-6yvv: Condensin complex from S.cerevisiae ATP-free apo bridged state
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-10953:
Condensin complex from S.cerevisiae ATP-free apo bridged state: focused refinement on arm segment
Method: EM (single particle) / Resolution: 7.8 Å

EMDB-10954:
Condensin complex from S.cerevisiae ATP-free apo bridged state: overall map
Method: EM (single particle) / Resolution: 9.1 Å

EMDB-10964:
Rod-shaped arm segment of the S.cerevisiae condensin complex in presence of ATP
Method: EM (single particle) / Resolution: 8.2 Å

Source
  • Saccharomyces cerevisiae S288C (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • Saccharomyces cerevisiae (brewer's yeast)
KeywordsCELL CYCLE / Condensin chromosome condensation SMC protein / essential for the functional organization of genomes

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