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TitleSubstrate recognition by human separase.
Journal, issue, pagesSci Adv, Vol. 11, Issue 46, Page eady9807, Year 2025
Publish dateNov 14, 2025
AuthorsJun Yu / Sophia Schmidt / Margherita Botto / Kitaik Lee / Chloe M Ghent / Jonah M Goodfried / Andrew Howe / Francis J O'Reilly / David O Morgan / Andreas Boland /
PubMed AbstractThe cohesin complex encircles sister chromatids in early mitosis. At anaphase onset, sister separation is triggered by the proteolytic cleavage of the cohesin subunit SCC1/RAD21 by separase. SCC1 ...The cohesin complex encircles sister chromatids in early mitosis. At anaphase onset, sister separation is triggered by the proteolytic cleavage of the cohesin subunit SCC1/RAD21 by separase. SCC1 contains two cleavage sites, where cleavage is stimulated by SCC1 phosphorylation. Substrate recognition and cleavage are only partly understood. Here, we determined structures of human separase in apo- or substrate-bound forms that, together with biochemical analysis, provide critical insights into separase cleavage regulation. We verify the first SCC1 cleavage site and reassign the second. We show that substrates, including separase autocleavage sites and the two SCC1 cleavage sites, interact with docking sites in separase, including five phosphate-binding sites. We also describe the interaction between the cohesin subunit SA1/SA2 and separase, which promotes cleavage at the second SCC1 site. Using cross-linking mass spectrometry and cryo-electron microscopy, we propose how cohesin is targeted by human separase. Our work provides an extensive functional and structural framework that explains a key event in cell division.
External linksSci Adv / PubMed:41223273 / PubMed Central
MethodsEM (single particle)
Resolution2.77 - 3.45 Å
Structure data

52288

9hm7

EMDB-52288, PDB-9hm7:
Cryo-EM structure of apo human separase with the mutation C2029S
Method: EM (single particle) / Resolution: 3.1 Å

52290

9hma

EMDB-52290, PDB-9hma:
Cryo-EM structure of apo human separase
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-52291: Focus-refined map (mask 1) of human separase bound to SCC1 (310-550 aa) and SA2
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-52294: Focus-refined map (mask 2) of human separase bound to SCC1 (310-550 aa) and SA2
Method: EM (single particle) / Resolution: 3.45 Å

EMDB-52295: Consensus map of human separase bound to SCC1 (310-550 aa) and SA2
Method: EM (single particle) / Resolution: 3.4 Å

52297

9hms

EMDB-52297, PDB-9hms:
Cryo-EM structure of human separase bound to SCC1 (310-550 aa) and SA2
Method: EM (single particle) / Resolution: 3.4 Å

52298

9hmv

EMDB-52298, PDB-9hmv:
Cryo-EM structure of SA2-SCC1 complex at 2.9 angstrom
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-52300: Focus-refined map of human separase bound to SCC1 (310-550 aa) with a mask on TPR-like domain and SPD
Method: EM (single particle) / Resolution: 2.77 Å

EMDB-52301: Focus-refined map of human separase bound to SCC1 (310-550 aa) with a mask on HEAT-repeat domain
Method: EM (single particle) / Resolution: 3.45 Å

EMDB-52302: Consensus map of human separase bound to SCC1 (310-550 aa)
Method: EM (single particle) / Resolution: 2.84 Å

52303

9hn0

EMDB-52303, PDB-9hn0:
Cryo-EM structure of human separase bound to SCC1 (310-550 aa)
Method: EM (single particle) / Resolution: 2.8 Å

52306

9hn4

EMDB-52306, PDB-9hn4:
Cryo-EM structure of human separase bound to phosphorylated SCC1 (310-550 aa)
Method: EM (single particle) / Resolution: 2.93 Å

52307

9hn5

EMDB-52307, PDB-9hn5:
Cryo-EM structure of human separase bound to phosphorylated SCC1 (100-320 aa)
Method: EM (single particle) / Resolution: 2.96 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / Separase / SCC1 / RAD21 / protease / chromosome segregation / Auto-cleavage / SA1/2 / cohesin

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