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5HT - Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3

ABSTRACT: we provide evidence for a new class of histone posttranslational modification (PTM): serotonylation.

OTHER RELATED OMICS DATASETS IN: GSE117910

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: henrik molina

LAB HEAD: Ian Maze

PROVIDER: PXD008106 | Pride | 2018-12-19

REPOSITORIES: Pride

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			Action	DRS
	MS151863QE_ian_allis_Light_5HT_minus-minus_a.raw	Raw
	MS151863QE_ian_allis_Light_5HT_plus-minus_a.raw	Raw
	MS151863QE_ian_allis_Light_5HT_plus-plus_a.raw	Raw
	MS184260LUM_ian_maze_H3-1_a.msf	Msf
	MS184260LUM_ian_maze_H3-1_a.raw	Raw

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Publications

Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3.

Farrelly Lorna A LA Thompson Robert E RE Zhao Shuai S Lepack Ashley E AE Lyu Yang Y Bhanu Natarajan V NV Zhang Baichao B Loh Yong-Hwee E YE Ramakrishnan Aarthi A Vadodaria Krishna C KC Heard Kelly J KJ Erikson Galina G Nakadai Tomoyoshi T Bastle Ryan M RM Lukasak Bradley J BJ Zebroski Henry H Alenina Natalia N Bader Michael M Berton Olivier O Roeder Robert G RG Molina Henrik H Gage Fred H FH Shen Li L Garcia Benjamin A BA Li Haitao H Muir Tom W TW Maze Ian I

Nature 20190313 7749

Chemical modifications of histones can mediate diverse DNA-templated processes, including gene transcription<sup>1-3</sup>. Here we provide evidence for a class of histone post-translational modification, serotonylation of glutamine, which occurs at position 5 (Q5ser) on histone H3 in organisms that produce serotonin (also known as 5-hydroxytryptamine (5-HT)). We demonstrate that tissue transglutaminase 2 can serotonylate histone H3 tri-methylated lysine 4 (H3K4me3)-marked nucleosomes, resulting ...[more]

PMID: 30867594

Similar Datasets

5HT - Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3

Project description:we provide evidence for a new class of histone posttranslational modification (PTM): serotonylation.

2023-12-04 | MSV000093567 | MassIVE

Cse4 ChIP-chip

Project description:In order to take an unbiased approach and discover all the locations of Cse4 in the genome, we utilized formaldehyde crosslinking and immunoprecipitation followed by hybridization to DNA microarrays. We analyzed the location of Cse4 in three different strains; one in which the endogenous Cse4 is tagged with 12Myc epitopes (Cse4-12Myc), and one which contained both the endogenous Cse4 (untagged) and an ectopic copy of Cse4-12Myc expressed from the GAL1-10 promoter (pGAL1-10-Cse4-12Myc), and one in which Cse4 is tagged with 3HA epitopes (Cse4-3HA). ChIP-chip was performed using custom microarrays, to look at the genome-wide localization of the centromeric histone variant Cse4. Biological replicates were performed for each Cse4 epitope-tagged strain

2009-08-28 | E-GEOD-17481 | biostudies-arrayexpress

Histone serotonylation is a permissive modification that enhances TFIID binding to H3K4me3.

Project description:Chemical modifications of histones can mediate diverse DNA-templated processes, including gene transcription1-3. Here we provide evidence for a class of histone post-translational modification, serotonylation of glutamine, which occurs at position 5 (Q5ser) on histone H3 in organisms that produce serotonin (also known as 5-hydroxytryptamine (5-HT)). We demonstrate that tissue transglutaminase 2 can serotonylate histone H3 tri-methylated lysine 4 (H3K4me3)-marked nucleosomes, resulting in the presence of combinatorial H3K4me3Q5ser in vivo. H3K4me3Q5ser displays a ubiquitous pattern of tissue expression in mammals, with enrichment observed in brain and gut, two organ systems responsible for the bulk of 5-HT production. Genome-wide analyses of human serotonergic neurons, developing mouse brain and cultured serotonergic cells indicate that H3K4me3Q5ser nucleosomes are enriched in euchromatin, are sensitive to cellular differentiation and correlate with permissive gene expression, phenomena that are linked to the potentiation of TFIID4-6 interactions with H3K4me3. Cells that ectopically express a H3 mutant that cannot be serotonylated display significantly altered expression of H3K4me3Q5ser-target loci, which leads to deficits in differentiation. Taken together, these data identify a direct role for 5-HT, independent from its contributions to neurotransmission and cellular signalling, in the mediation of permissive gene expression.

| S-EPMC6557285 | biostudies-literature

Glutamine 5 serotonylation on histone H3 is a permissive modification that functions combinatorialy with H3K4me3 to potentiate TFIID interactions

Project description:Chemical modifications of histone proteins, along with the ?writers,? ?erasers? and ?readers? of these modifications, are capable of mediating a diverse set of DNA-templated processes including gene transcription1-7. Here, we provide evidence for a new class of histone posttranslational modification (PTM), serotonylation of glutamine, which occurs at position 5 (Q5ser) on histone H3 in serotonin (5-hydroxytryptamine, 5-HT) producing organisms. We demonstrate that the tissue Transglutaminase 2 (TGM2) enzyme, a transamidase that is both necessary and sufficient to deposit the mark, can serotonylate H3 on lysine 4 tri-methylated (H3K4me3) nucleosomes resulting in the presence of combinatorial H3K4me3Q5ser in vivo. H3K4me3Q5ser displays a ubiquitous pattern of tissue expression in mammals, with predicted enrichment observed in brain and gut, two organ systems responsible for the bulk of 5-HT production. Genome-wide analyses of its enrichment in human serotonergic neurons, developing mouse brain and cultured serotonergic cells, using an H3K4me3Q5ser specific antibody, indicate that the mark is enriched in euchromatin, is sensitive to cellular differentiation and correlates with permissive gene expression, phenomena that are linked to the mark?s potentiation of TFIID8-10 interactions with H3K4me3. Cells ectopically expressing an H3 mutant that cannot be serotonylated display significantly altered expression of H3K4me3Q5ser target loci leading to deficits in differentiation. Taken together, these data identify a direct role for 5-HT, independent from its contributions to neurotransmission and cellular signaling, in the mediation of permissive gene expression in mammalian cells, and further define its biophysical activities as a putative co-regulator of TFIID recruitment to H3K4me3 marked chromatin.

2018-12-18 | GSE106495 | GEO

BiTS Chromatin Immunoprecipitation of H3K4me3 and H3K27ac in Drosophila melanogaster differentiating cardiomyocytes

Project description:Here we improved BiTS-ChIP (Bonn et al, Nature Protocols 7, 978-994 (2012)) to identify active enhancer and promoter elements genome wide in the 104 cardiomyocytes that constitute the Drosophila heart tube and represents only ~0.5% of the total cell content of the embryo. A transgenic Drosophila strain expressing nuclear GFP under the control of a cardiac specific enhancer (TinC*>GFP) was used for staged embryo collections at stages 13-14 (10-13h of development). After embryo fixation and dissociation, intact fixed nuclei were fluorescent labelling. Purification of this rare nuclear population was achieved by a two-step sorting procedure, yielding ~98% purity. Chromatin was extracted and used for immunoprecipitation and sequencing (ChIP-seq) to analyze chromatin modifications at promoters (H3K4me3 and H3K27ac) and enhancers (H3K27ac). Two independent biological replicates (from FACS sorting, chromatin preparations and ChIP-Seq) were performed for each mark and sequenced using Illumina HiSeq.

2017-01-10 | E-MTAB-4584 | biostudies-arrayexpress

Glutamine 5 serotonylation on histone H3 is a permissive modification that functions combinatorialy with H3K4me3 to potentiate TFIID interactions

Project description:Glutamine 5 serotonylation on histone H3 is a permissive modification that functions combinatorialy with H3K4me3 to potentiate TFIID interactions

| PRJNA417049 | ENA

Serotonin transporter-dependent histone serotonylation in placenta contributes to the neurodevelopmental transcriptome [RNA-seq]

Project description:Brain development requires appropriate regulation of serotonin (5-HT) signaling from distinct tissue sources across embryogenesis. At the maternal-fetal interface, the placenta is thought to be an important contributor of offspring brain 5-HT and is critical to overall fetal health. Yet, how placental 5-HT is acquired, and the mechanisms through which 5-HT influences placental functions, are not well understood. Recently, our group identified a novel epigenetic role for 5-HT, in which 5-HT can be added to histone proteins to regulate transcription, a process called H3 serotonylation. Here, we show that H3 serotonylation undergoes dynamic regulation during placental development, corresponding to gene expression changes that are known to influence key metabolic processes. Using transgenic mice, we demonstrate that placental H3 serotonylation largely depends on 5-HT uptake by the serotonin transporter (Sert/Slc6a4). Sert deletion robustly reduces enrichment of H3 serotonylation across the placental genome, and disrupts neurodevelopmental gene networks in offspring brain tissues. Thus, these findings suggest a novel role for H3 serotonylation in coordinating placental transcription at the intersection of maternal physiology and offspring brain development.

2024-01-23 | GSE246539 | GEO

Serotonin transporter-dependent histone serotonylation in placenta contributes to the neurodevelopmental transcriptome [ChIP-seq]

2024-01-23 | GSE246538 | GEO

Genome-wide maps of WT and over-expressing CenH3/CENP-A in Human HeLa S3 cells

Project description:Centromeres are essential to ensure proper chromosome segregation in eukaryotes. Their definition relies on the presence of a centromere-specific H3 histone variant CenH3, known as CENP-A in mammals. Its overexpression in aggressive cancers raises questions concerning its effect on chromatin dynamics and contribution to tumorigenesis. We find that CenH3 overexpression in human cells leads to ectopic enrichment at sites of active histone turnover. Furthermore, in over-expressing conditions, we see the formation of a novel heterotypic particle (CenH3-H4/H3.3-H4) that occludes CTCF binding, but this occlusion has only a minor effect on gene expression. Ectopic localization and CTCF occlusion depends on the H3.3 chaperone DAXX, rather than its dedicated chaperone HJURP. This DAXX-dependent occlusion also occurs in naturally overexpressing cancer cells. Furthermore, our cellular model reveals a DAXX-dependent survival advantage when challenged by DNA damage. Our findings illustrate how changes in histone variant levels can disrupt chromatin dynamics in disease and provides a possible mechanism for cell resistance to anti-cancer treatments. Examination of CenH3 ChIP-seq and RNA-seq transcriptional programs in two conditions - WT and CenH3 over-expressing.

2014-02-12 | E-GEOD-42951 | biostudies-arrayexpress

Histone peptide pull-down H3K4me0-3 +/- H3Q5ser

Project description:The interactome to H3 peptides in different H3K4 methylation states and its change upon H3Q5 serotonylation was determined by performing peptide pull-down followed by qMS. Streptaviding beads, saturated with biotinylated H3 peptides in all possible H3K4 methylation states and with presence and absence of H3Q5 serotonylation.

2025-06-10 | PXD062109 | Pride

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