ArticleMolecular & cellular proteomics : MCP2014
Quantitative proteomics reveals histone modifications in crosstalk with H3 lysine 27 methylation.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Exploration of the Nuclear Proteomes in the CiliateMicroorganisms · 2023Article
- Orchestration of H3K27 methylation: mechanisms and therapeutic implication.Cellular and molecular life sciences : CMLS · 2018Review
- Specific Acetylation Patterns of H2A.Z Form Transient Interactions with the BPTF Bromodomain.Biochemistry · 2017Article
- Quantitative proteomic analysis of histone modifications in decitabine sensitive and resistant leukemia cell lines.Clinical proteomics · 2016Article
- Quantification of histone modifications by parallel-reaction monitoring: a method validation.Analytical chemistry · 2015Article
- Bioinformatic and proteomic analysis of bulk histones reveals PTM crosstalk and chromatin features.Journal of proteome research · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Methylation at histone H3 lysine 27 (H3K27me) is an evolutionarily conserved epigenetic mark associated with transcriptional repression and replication elongation. We have previously shown that in Tetrahymena thermophila, a unicellular eukaryote, the histone methyltransferases (HMTs) TXR1 and EZL2 are primarily responsible for H3K27 mono-methylation (H3K27me1) and di-/tri-methylation (H3K27me2/3), respectively. Using (15)N metabolically labeled histones as the internal reference, we quantified global changes in histone post-translational modifications in ΔTXR1 and ΔEZL2 cells, to systematically identify potential crosstalk between H3K27 methylation and other PTMs across all four core histones as well as their variants. Most prominently, we observed hyper-acetylation of histones H2A, H2A.Z, and H4 in their N-terminal domains in response to decreased H3K27 methylation. We also provide additional evidence implicating hyper-acetylation in the DNA damage response pathway in replication-defective ΔTXR1 cells, in apparent contrast to the transcriptional role of hyper-acetylation in ΔEZL2 cells.
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