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TitleAPC/C-mediated ubiquitylation of extranucleosomal histone complexes lacking canonical degrons.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 2561, Year 2025
Publish dateMar 15, 2025
AuthorsAleksandra Skrajna / Tatyana Bodrug / Raquel C Martinez-Chacin / Caleb B Fisher / Kaeli A Welsh / Holly C Simmons / Eyla C Arteaga / Jake M Simmons / Mohamed A Nasr / Kyle M LaPak / Anh Nguyen / Mai T Huynh / Isabel Fargo / Joshua G Welfare / Yani Zhao / David S Lawrence / Dennis Goldfarb / Nicholas G Brown / Robert K McGinty /
PubMed AbstractNon-degradative histone ubiquitylation plays a myriad of well-defined roles in the regulation of gene expression and choreographing DNA damage repair pathways. In contrast, the contributions of ...Non-degradative histone ubiquitylation plays a myriad of well-defined roles in the regulation of gene expression and choreographing DNA damage repair pathways. In contrast, the contributions of degradative histone ubiquitylation on genomic processes has remained elusive. Recently, the APC/C has been shown to ubiquitylate histones to regulate gene expression in pluripotent cells, but the molecular mechanism is unclear. Here we show that despite directly binding to the nucleosome through subunit APC3, the APC/C is unable to ubiquitylate nucleosomal histones. In contrast, extranucleosomal H2A/H2B and H3/H4 complexes are broadly ubiquitylated by the APC/C in an unexpected manner. Using a combination of cryo-electron microscopy (cryo-EM) and biophysical and enzymatic assays, we demonstrate that APC8 and histone tails direct APC/C-mediated polyubiquitylation of core histones in the absence of traditional APC/C substrate degron sequences. Taken together, our work implicates APC/C-nucleosome tethering in the degradation of diverse chromatin-associated proteins and extranucleosomal histones for the regulation of transcription and the cell cycle and for preventing toxicity due to excess histone levels.
External linksNat Commun / PubMed:40089476 / PubMed Central
MethodsEM (single particle)
Resolution3.9 Å
Structure data

48928

9n9r

EMDB-48928: Cryo-EM map of APC/C-CDC20-UBE2C-H2A/H2B crosslinked complex
PDB-9n9r: Model of APC/C-CDC20-UBE2C from H2A/H2B-bound complex
Method: EM (single particle) / Resolution: 3.9 Å

48984

9n9s

EMDB-48984: Cryo-EM map of APC/C-CDC20-UBE2C-H3/H4 crosslinked complex
PDB-9n9s: Model of APC/C-CDC20-UBE2C from H3/H4-bound complex
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / ubiquitin ligase / histone / chromatin / ubiquitin / complex

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