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Site‐specific human histone H3 methylation stability: fast K4me3 turnover
Author(s) -
Zheng Yupeng,
Tipton Jeremiah D.,
Thomas Paul M.,
Kelleher Neil L.,
Sweet Steve M. M.
Publication year - 2014
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201400060
Subject(s) - histone , methylation , histone h3 , transcription (linguistics) , nucleosome , histone methylation , biology , epigenetics , microbiology and biotechnology , dna methylation , genetics , gene expression , dna , gene , linguistics , philosophy
We employ stable‐isotope labeling and quantitative mass spectrometry to track histone methylation stability. We show that H3 trimethyl K9 and K27 are slow to be established on new histones and slow to disappear from old histones, with half‐lives of multiple cell divisions. By contrast, the transcription‐associated marks K4me3 and K36me3 turn over far more rapidly, with half‐lives of 6.8 h and 57 h, respectively. Inhibition of demethylases increases K9 and K36 methylation, with K9 showing the largest and most robust increase. We interpret different turnover rates in light of genome‐wide localization data and transcription‐dependent nucleosome rearrangements proximal to the transcription start site.