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TitleArchitecture and subunit arrangement of the complete Saccharomyces cerevisiae COMPASS complex.
Journal, issue, pagesSci Rep, Vol. 8, Issue 1, Page 17405, Year 2018
Publish dateNov 27, 2018
AuthorsYanxing Wang / Zhanyu Ding / Xiangyang Liu / Yu Bao / Min Huang / Catherine C L Wong / Xiaoyu Hong / Yao Cong /
PubMed AbstractMethylation of histone H3 lysine 4 (H3K4) is catalyzed by the multi-component COMPASS or COMPASS-like complex, which is highly conserved from yeast to human, and plays essential roles in gene ...Methylation of histone H3 lysine 4 (H3K4) is catalyzed by the multi-component COMPASS or COMPASS-like complex, which is highly conserved from yeast to human, and plays essential roles in gene expression and transcription, cell cycle progression, and DNA repair. Here we present a cryo-EM map of the complete S. cerevisiae COMPASS complex. Through tag or Fab labeling strategy combined with cryo-EM 3D reconstruction and cross-linking and mass spectrometry (XL-MS) analysis, we uncovered new information on the subunit arrangement: Cps50, Cps35, and Cps30 were determined to group together to form the face region in the head of the complex, and Cps40 and the N-terminal portion of Set1 reside on the top of the head. Our map reveals the location of the active center and a canyon in the back of the head. Together, our study provides the first snapshot of the complete architecture of yeast COMPASS and a picture of its subunit interaction network, which could facilitate our understanding of the COMPASS machinery and its functionality.
External linksSci Rep / PubMed:30479350 / PubMed Central
MethodsEM (single particle)
Resolution10.0 Å
Structure data

EMDB-9694:
The complete structure of yeast COMPASS
Method: EM (single particle) / Resolution: 10.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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