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An intrinsically disordered region of histone demethylase KDM5A regulates catalysis through interactions with the nucleosomal acidic patch and DNA

ABSTRACT: KDM5A lysine demethylase conformation was probed by BS3 crosslinking in the presence and absence of DNA. Crosslinked proteins were reduced, alkylated with iodoacetamide, trypsin digest, and labeled with TMT6plex reagent prior to mixing and acquisition on an Orbitrap Exploris equiped with a FAIMS source. Three biological replicates are included split over multipe technical replicates and/or SEC fractions. The SampleKey.txt file explains the labeling scheme.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Danica Galonic Fujimori

PROVIDER: MSV000097094 | MassIVE | Mon Feb 10 14:49:00 GMT 2025

SECONDARY ACCESSION(S): PXD055029

REPOSITORIES: MassIVE

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Publications

An Intrinsically Disordered Region of Histone Demethylase KDM5A Activates Catalysis Through Interactions With the Nucleosomal Acidic Patch and DNA.

Palla Ali M AM Lin Chien-Chu CC Trnka Michael J MJ Leao Emme M EM Petronikolou Nektaria N Burlingame Alma L AL McGinty Robert K RK Fujimori Danica Galonić DG

Journal of molecular biology 20250620 19

Lysine demethylase 5A (KDM5A) plays a key role in the regulation of chromatin accessibility by catalyzing the removal of trimethyl marks on histone H3K4 (H3K4me3). KDM5A is also an oncogenic driver, with overexpression of KDM5A observed in various cancers, including breast, lung, and ovarian cancer. Past studies have characterized the functions of KDM5A domains, including KDM5A interactions with the histone H3 tail, but have yet to identify the broader mechanisms that drive KDM5A binding to the ...[more]

PMID: 40545232

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BS3

Project description:BS3 Raw sequence reads

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