ArticleScientific reports2018
Architecture and subunit arrangement of the complete Saccharomyces cerevisiae COMPASS complex.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- A systematic interactome ofeLife · 2026Article
- An immobilized antibody-based affinity grid strategy for on-grid purification of target proteins enables high-resolution cryo-EM.Communications biology · 2024Article
- The Core Complex of Yeast COMPASS and Human Mixed-Lineage Leukemia (MLL), Structure, Function, and Recognition of the Nucleosome.Sub-cellular biochemistry · 2024Review
- Review
- Diverse and dynamic forms of gene regulation by the S. cerevisiae histone methyltransferase Set1.Current genetics · 2023Review
- Histone 3 lysine 4 monomethylation supports activation of transcription in S. cerevisiae during nutrient stress.Current genetics · 2022Article
- Distinct architecture and composition of mouse axonemal radial spoke head revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural Biology in the Multi-Omics Era.Journal of chemical information and modeling · 2020Article
- The Set1 N-terminal domain and Swd2 interact with RNA polymerase II CTD to recruit COMPASS.Nature communications · 2020Article
- Interpretation of medium resolution cryoEM maps of multi-protein complexes.Current opinion in structural biology · 2019Review
- Advances in domain and subunit localization technology for electron microscopy.Biophysical reviews · 2019Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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