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TitleStructural basis of nucleosome deubiquitination by the bidentate Calypso/Asx complex.
Journal, issue, pagesiScience, Vol. 29, Issue 3, Page 114958, Year 2026
Publish dateMar 20, 2026
AuthorsChi Wang / Fahui Sun / Heyu Zhao / Nan Zhang / Jiali Guan / Yuxing Zhou / Wentong Shuai / Hui Zheng / Jun He /
PubMed AbstractThe Polycomb repressive complex 1 (PRC1) and PR-DUB constitute a canonical pair of histone-modifying enzymes that deposit and remove monoubiquitinated H2A at lysine 119 (H2AK119ub1), serving as a ...The Polycomb repressive complex 1 (PRC1) and PR-DUB constitute a canonical pair of histone-modifying enzymes that deposit and remove monoubiquitinated H2A at lysine 119 (H2AK119ub1), serving as a model of dynamic epigenetic regulation. In humans, PR-DUB, composed of BAP1 and ASXL1, functions as a monomeric complex, while the homolog Calypso/Asx forms a bidentate dimer (Calypso: Asx) with an unclear chromatin engagement mechanism. Here, we present its cryo-EM structure bound to a nucleosome, revealing the molecular basis of interaction. Surprisingly, only one Calypso/Asx unit engages the nucleosome in a conformation similar to human BAP1/ASXL1, while the second remains disengaged. Structural and biochemical analysis of the positively charged Calypso C terminus suggests a "spreading" potential of the bidentate complex along chromatin, which was validated using nucleosome arrays. These findings support a model in which the bidentate Calypso/Asx complex enables processive deubiquitination along chromatin via alternating or cooperative engagement.
External linksiScience / PubMed:41782825 / PubMed Central
MethodsEM (single particle)
Resolution5.9 Å
Structure data

64748

9v33

EMDB-64748, PDB-9v33:
Calypso/Asx/NCP-ub complex
Method: EM (single particle) / Resolution: 5.9 Å

Source
  • drosophila melanogaster (fruit fly)
  • xenopus laevis (African clawed frog)
  • homo sapiens (human)
  • escherichia coli (E. coli)
KeywordsTRANSCRIPTION/DNA / PR-DUB / Calypso / Polycomb / TRANSCRIPTION-DNA complex

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