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XL-MS analysis of COMPASS complex and its interactions with nucleosome

ABSTRACT: This project presents cross-linking mass spectrometry (XL-MS) data of the COMPASS complex from Saccharomyces cerevisiae. COMPASS (Complex Proteins Associated with Set1) is a conserved histone H3 lysine 4 (H3K4) methyltransferase essential for transcriptional regulation, cell cycle progression, and chromatin signaling. The Cps35 subunit (also known as Swd2) is a critical component for COMPASS stability and its interaction with methylated H3K4. To dissect the architectural organization and the role of Cps35 in COMPASS-nucleosome interaction, we performed XL-MS analysis on four distinct conditions: (1) intact COMPASS complex, (2) COMPASS lacking the Cps35 subunit (COMPASS Δcps35), (3) COMPASS bound to nucleosome, and (4) COMPASS Δcps35 bound to nucleosome. All protein complexes were overexpressed in yeast and purified via TAP-tag affinity purification. This dataset includes raw MS files, search engine outputs, and identified cross-linked peptides for each condition .These data provide structural insights into the subunit interaction network of COMPASS and the molecular role of Cps35 in mediating COMPASS-nucleosome engagement.

ORGANISM(S): Saccharomyces Cerevisiae

SUBMITTER: Yao Cong

PROVIDER: PXD077644 | iProX | Sun Apr 26 00:00:00 BST 2026

REPOSITORIES: iProX

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