Mass spectrometry-based profiling of single-cell histone post-translational modifications to dissect chromatin heterogeneity.

ABSTRACT: Single-cell proteomics confidently quantifies cellular heterogeneity, however quantification of post-translational modifications, such as those deposited on histone proteins, remains elusive. Here, we develop a robust mass spectrometry-based method for the unbiased analysis of single-cell histone post-translational modifications (sc-hPTM). sc-hPTM identifies both single- and combinatorial histone post-translational modifications (67 peptidoforms in total), which includes nearly all frequently studied histone post-translational modifications with comparable reproducibility to traditional bulk experiments. As a proof of concept, we treat cells with sodium butyrate, a histone deacetylase inhibitor, and demonstrate that our method can i) distinguish between treated and untreated cells, ii) ide

SUBMITTER: Cutler R 

PROVIDER: S-EPMC12700877 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature