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Decoding the protein composition of whole nucleosomes with Nuc-MS

by Piunti Andrea , Iwanaszko Marta , Cheek, Marcus A , Kelleher, Neil L , Meiners, Matthew J , Lee, Alexander S , Michael-Christopher, Keogh , Howard, Sarah A , Morgan, Marc A , Shilatifard Ali , Burg, Jonathan M , Jooß, Kevin , Kafader, Jared O , Schachner, Luis F

in Blurring / Chromatin / Decoding / DNA methylation / Epigenetics / Histone H3 / Histones / Immunoprecipitation / Mass spectrometry / Mass spectroscopy / Nucleosomes / Occupancy / Peptides / Post-translation / Protein composition / Proteins / Translation

2021

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Decoding the protein composition of whole nucleosomes with Nuc-MS

2021

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2021

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Journal Article

Decoding the protein composition of whole nucleosomes with Nuc-MS

Piunti Andrea,

Iwanaszko Marta,

Cheek, Marcus A,

Kelleher, Neil L,

Meiners, Matthew J,

Lee, Alexander S,

Michael-Christopher, Keogh,

Howard, Sarah A,

Morgan, Marc A,

Shilatifard Ali,

Burg, Jonathan M,

Jooß, Kevin,

Kafader, Jared O,

Schachner, Luis F

2021

Overview

Current proteomic approaches disassemble and digest nucleosome particles, blurring readouts of the ‘histone code’. To preserve nucleosome-level information, we developed Nuc-MS, which displays the landscape of histone variants and their post-translational modifications (PTMs) in a single mass spectrum. Combined with immunoprecipitation, Nuc-MS quantified nucleosome co-occupancy of histone H3.3 with variant H2A.Z (sixfold over bulk) and the co-occurrence of oncogenic H3.3K27M with euchromatic marks (for example, a >15-fold enrichment of dimethylated H3K79me2). Nuc-MS is highly concordant with chromatin immunoprecipitation-sequencing (ChIP-seq) and offers a new readout of nucleosome-level biology.Nuc-MS makes use of top–down mass spectrometry in ‘native’ mode to quantitatively interrogate histone proteoforms and their post-translational modifications in a single experiment.

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Nature Publishing Group

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