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-Structure paper
Title | Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3. |
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Journal, issue, pages | Elife, Vol. 9, Year 2020 |
Publish date | Sep 15, 2020 |
Authors | James E Collier / Byung-Gil Lee / Maurici Brunet Roig / Stanislav Yatskevich / Naomi J Petela / Jean Metson / Menelaos Voulgaris / Andres Gonzalez Llamazares / Jan Löwe / Kim A Nasmyth / |
PubMed Abstract | In addition to extruding DNA loops, cohesin entraps within its SMC-kleisin ring (S-K) individual DNAs during G1 and sister DNAs during S-phase. All three activities require related hook-shaped ...In addition to extruding DNA loops, cohesin entraps within its SMC-kleisin ring (S-K) individual DNAs during G1 and sister DNAs during S-phase. All three activities require related hook-shaped proteins called Scc2 and Scc3. Using thiol-specific crosslinking we provide rigorous proof of entrapment activity in vitro. Scc2 alone promotes entrapment of DNAs in the E-S and E-K compartments, between ATP-bound engaged heads and the SMC hinge and associated kleisin, respectively. This does not require ATP hydrolysis nor is it accompanied by entrapment within S-K rings, which is a slower process requiring Scc3. Cryo-EM reveals that DNAs transported into E-S/E-K compartments are 'clamped' in a sub-compartment created by Scc2's association with engaged heads whose coiled coils are folded around their elbow. We suggest that clamping may be a recurrent feature of cohesin complexes active in loop extrusion and that this conformation precedes the S-K entrapment required for sister chromatid cohesion. |
External links | Elife / PubMed:32930661 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.4 Å |
Structure data | EMDB-11585, PDB-6zz6: |
Chemicals | ChemComp-ATP: ChemComp-MG: |
Source |
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Keywords | CELL CYCLE / SMC / cohesin / DNA |