MassIVE MSV000097094

Partial Public PXD055029

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

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Description

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. [doi:10.25345/C5513V75F] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: KDM5A, lysine demethylase, BS3 crosslinking, quantitative crosslinking ; DatasetType:Proteomics

Contact

Principal Investigators:
(in alphabetical order) 		Danica Galonic Fujimori, University of California San Francisco, USA
Submitting User: mtrnka

Publications

Palla AM, Lin CC, Trnka MJ, Leao EM, Petronikolou N, Burlingame AL, McGinty RK, Fujimori DG.
An intrinsically disordered region of histone demethylase KDM5A activates catalysis through interactions with the nucleosomal acidic patch and DNA.
J Mol Biol. Epub 2025 Jun 20.

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