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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.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Ian Maze

PROVIDER: MSV000093567 | MassIVE | Mon Dec 04 15:54:00 GMT 2023

SECONDARY ACCESSION(S): PXD008106

REPOSITORIES: MassIVE

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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.

2018-12-19 | PXD008106 | Pride

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

Project description:We report the identification of 67 previously undescribed histone modifications, increasing the current number of known histone marks by about 70%. We further investigated one of the marks, lysine crotonylation (Kcr), confirming that it represents an evolutionarily-conserved histone posttranslational modification. The unique structure and genomic localization of histone Kcr suggest that it is mechanistically and functionally different from histone lysine acetylation (Kac). Specifically, in both human somatic and mouse male germ cell genomes, histone Kcr marks either active promoters or potential enhancers. In male germinal cells immediately following meiosis, Kcr is enriched on sex chromosomes and specifically marks testis-specific genes, including a significant proportion of X-linked genes that escape sex chromosome inactivation in haploid cells. These results therefore dramatically extend the repertoire of histone PTM sites and designate Kcr as a specific mark of active sex chromosome-linked genes in postmeiotic male germ cells. 2 histone marks (pan-lysine acetylation and pan-lysine crotonylation) were studied in 1 human cell type and 2 mouse cell types using ChIP-Seq. Input was sequenced for each cell type as a control. Pan-anti_Kac and pan-anti_Kcr antibodies were custom developed with PTM BioLab, Co., Ltd (Chicago, IL).

2011-10-06 | E-GEOD-32663 | biostudies-arrayexpress

Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification

2011-10-06 | GSE32663 | GEO

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

Deduction of proportional contributions of histone-modification-related DNA from various tissues in plasma

Project description:Deduction of proportional contributions of histone-modification-related DNA from various tissues in plasma

| EGAS00001006503 | EGA

Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

Project description:Chromatin is decorated with diverse histone posttranslational modifications (PTMs) that are involved in regulating chromatin structure and dynamics during various DNA-associated processes such as gene transcription, DNA replication and DNA damage repair. Here, we combine a chemical reporter with mass spectrometry to identify a new class of histone PTM, lysine glutarylation (Kglu), occurring at 27 lysine residues on human core histones. The characterization of an evolutionarily conserved Kglu mark at histone H4 lysine 91 (H4K91glu) using a semisynthetic glutarylated protein reveals that this negatively charged modification greatly destabilizes nucleosome by weakening the interactions between histone H2A/H2B dimers and H3/H4 tetramer in vitro. The replacement of H4K91 by glutamic acid in S. cerevisiae to mimic glutarylation influences chromatin structure and thereby results in a global up-regulation of transcription and defects in cell cycle progression, DNA damage repair and telomere silencing in vivo. In mammalian cells, H4K91glu is mainly enriched at promoter regions of highly expressed genes. A down-regulation of H4K91glu is tightly associated with chromatin condensation during mitosis and in response to DNA damage. The cellular dynamics of H4K91glu is controlled by Sirt7 as a deglutarylase and KAT2A as a glutaryltransferase. This study designates a new histone mark (Kglu) as a new regulatory mechanism for chromatin dynamics.

2019-09-16 | GSE131807 | GEO

Multi-omics approaches for revealing the epigenetic regulation of histone H3.1 during spermatogonial stem cell differentiation in vitro

Project description:Epigenetic regulation, particularly histone post translational modification (PTM), participates in spermatogonial stem cells (SSCs) differentiation. However, prior research is still limited to a single PTM. Herein, we constructed over 100 histone H3.1 targeted modification peptides, in combination with histone H3.1 modification binding protein identification, and RNA-Seq. We identified 7 differentially expressed histone H3.1 modifications. In addition, we selected H3K9me2 and H3S10ph for subsequent biotinylating peptide pull-down experiments, and identified a series of transcription factors, such as, GTF2E2 and SUPT5H, which appear to be crucial for the early SSC differentiation process.

2023-03-01 | GSE222617 | GEO

Proper parental histone allocation is required for mouse embryonic stem cell differentiation and histone post-transcription modification inheritance

Project description:To understand whether parental histone PTM landscape plays roles in cell differentiation, we perturbed parental histone PTM allocation by mutating histone chaperone MCM2 on its histone binding domain (MCM2-2A mutation), disrupted only the histone transferring of MCM2 protein in mouse embryonic stem cells (ESCs). Combining single-cell transcriptomics and epigenomics with lineage barcoding, we found that MCM2-2A mutant ESCs cannot be fully differentiated to neuronal precursor cells (NPCs), causing by the redistribution of H3K27me3, and subsequently NPC related gene expression. Here, we show that the parental histone allocation plays an important role in the establishment of chromatin landscapes, altering ESC differentiational potential, shaping expression programs and cell heterogeneity.

2023-05-15 | GSE185271 | GEO

Global Identification of Protein PTMs in a Single-pass Database Search

Project description:Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify posttranslational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables Global PTM (G-PTM) identification by exclusively looking for curated PTMs, thereby avoiding the FDR penalty experienced during conventional variable modification searches. We identified nearly 2500 unique, high-confidence modified peptides comprising 31 different PTM types in single-pass database searches.

2015-07-31 | GSE59956 | GEO

histone modification signatures in mice melanoma progression

Project description:In the search for the biological mechanisms that underlie melanoma development, we have developed a cellular system that models tumor initiation and transformation from melanocytes to metastatic melanoma cells.. To evaluate histone PTM, we applied a workflow to globally detect histone PTM by mass spectrometry approaches allowing the interrogation of more than 40 PTMs sites and 200 PTMs combinations.

2021-09-09 | PXD019313 | Pride

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