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ProteomicsTwo DOT1 enzymes cooperatively mediate efficient ubiquitin-independent histone H3 lysine 76 tri-methylation in kinetoplastids
In higher eukaryotes, a single DOT1 histone H3 lysine 79 (H3K79) methyltransferase processively produces H3K79me2/me3 from me0 through histone H2B mono-ubiquitin interaction. The early-branched kinetoplastid Trypanosoma brucei harbors the essential H3K76 di-methyltransferase DOT1A and the non-essent...
ORGANISM(S): Trypanosoma Brucei (ncbitaxon:5691) 
2022-11-09 | MSV000090680 | MassIVE
MetabolomicsDisruption of Methionine Metabolism Drives Erythroid Cell Fate Reprogramming by Remodeling the H3K4me3 Landscape

Methionine cycle plays critical roles in cell fate determination by shaping epigenetic landscape, yet its function in human erythropoiesis remains undefined. Here, we show that disruption of methionine metabolism by compromising key enzyme adenosylhomocysteinase (AHCY) reshapes H3K4me3 landscape,...

2026-06-10 | MTBLS10469 | MetaboLights
ProteomicsQuantitative histone mass spectrometry identifies elevated histone H3 lysine 27 trimethylation in melanoma
Normal cell growth is characterized by a regulated epigenetic program that drives cellular activities such as gene transcription, DNA replication and DNA damage repair. Perturbation of this epigenetic program can lead to events such as mis-regulation of gene transcription and diseases such as cancer...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-07-22 | MSV000079979 | MassIVE
TranscriptomicsGate-Keeping transcription through histone H3 K42, a novel site of methylation in the yeast nucleosome core
A new site of methylation was identified on histone H3 K42 in Saccharomyces cerevisiae. Mutations were engineered at this site to mimic either a constitutively modified state, K42L, or a constitutively unmodified state, K42Q in addition to an alanine substitution. K42A. The effects of these mutation...
ORGANISM(S): Saccharomyces cerevisiae 
2010-05-27 | E-GEOD-13889 | biostudies-arrayexpress
ProteomicsIdentification of ubiquitination sites of purified histone H3
Histones modulate gene expression by chromatin compaction, regulating numerous processes such as differentiation. However, the mechanisms underlying histone degradation remain elusive. When compared with their differentiated counterparts, immortal human embryonic stem cells (hESCs) have a unique chr...
ORGANISM(S): Homo sapiens (Human) 
2020-06-01 | PXD018621 | Pride
Epigenetics Ubiquitination Histone h3 
TranscriptomicsHistone H3 lysine 4 acetylation-methylation dynamics define breast cancer subtypes [RNA-seq]
The onset and progression of breast cancer are linked to genetic and epigenetic changes that alter the normal programming of cells. Epigenetic modifications of DNA and histones contribute to chromatin structure that results in the activation or repression of gene expression. Several epigenetic pathw...
ORGANISM(S): Homo sapiens 
2016-02-10 | E-GEOD-75168 | biostudies-arrayexpress
ProteomicsMus musculus brown adipose tissue histone proteoforms
Histones were isolated from brown adipose tissue and liver from mice housed at 28, 22, or 8 C. Quantitative top- or middle-down approaches were used to quantitate histone H4 and H3.2 proteoforms. See published article for complimentary RNA-seq and RRBS datasets.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2023-06-05 | MSV000092105 | MassIVE
GenomicsHistone H3K4 Demethylation is Negatively Regulated by Histone H3 Acetylation in S. cerevisiae
Histone H3 lysine 4 tri-methylation (H3K4me3) is a hallmark of transcription initiation, but how H3K4me3 is demethylated during gene repression is poorly understood. Jhd2, a JmjC domain protein, was recently identified as the major H3K4me3 histone demethylase (HDM) in S. cerevisiae. While JHD2 is ...
ORGANISM(S): Saccharomyces cerevisiae 
2012-11-05 | E-GEOD-41424 | biostudies-arrayexpress
ProteomicsA Chemical Acetylation based Mass Spectrometry Platform for Histone Profiling
Here we present a strategy for the identification and quantitation of histone methylation that utilizes nondeuterated acetic anhydride to fully acetylate all free lysine residues prior to digestion with trypsin and analysis by LC-MS/MS.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000086146 | MassIVE
ProteomicsUnique Histone Proteoforms by Differential Top Down MS
H3.1 and H3.3 quadrupole isolated and fragmented by ETD and EThcD on an Orbitrap Fusion Lumos. Comparison of two cell lines.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2015-07-14 | MSV000079191 | MassIVE
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