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LC-MS/MS identification of Kbz sites on histones catalyzed by non-enzymatic and enzymatic ways.

ABSTRACT: Histone lysine benzoylation may occur by Gcn5-catalyzed and nonenzymatically ways in vivo. In this project, we identified several Kbz sites on Xenopus laevis octamer in the absence or presence Gcn5-Ada2 complex in vitro, respectively. The number 672 represents the data in the absence of Gcn5-Ada2, and the number 674 represents the data that in the presence of Gcn5-Ada2.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Duo Wang

LAB HEAD: Chen Yong

PROVIDER: PXD030110 | Pride | 2022-05-19

REPOSITORIES: Pride

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Global profiling of regulatory elements in the histone benzoylation pathway.

Wang Duo D Yan Fuxiang F Wu Ping P Ge Kexue K Li Muchun M Li Tingting T Gao Ying Y Peng Chao C Chen Yong Y

Nature communications 20220316 1

Lysine benzoylation (Kbz) is a recently discovered post-translational modification associated with active transcription. However, the proteins for maintaining and interpreting Kbz and the physiological roles of Kbz remain elusive. Here, we systematically characterize writer, eraser, and reader proteins of histone Kbz in S. cerevisiae using proteomic, biochemical, and structural approaches. Our study identifies 27 Kbz sites on yeast histones that can be regulated by cellular metabolic states. The ...[more]

PMID: 35296687

Similar Datasets

Lysine benzoylation - Here we report the identification and characterization of a histone mark, lysine benzoylation (Kbz). Our study identifies 22 Kbz sites on histones from HepG2 and RAW cells. This type of histone mark can be stimulated by sodium benzoate (SB), a FDA-approved drug and a widely used chemical food preservative, via generation of benzoyl CoA.

Project description:Here we report the identification and characterization of a histone mark, lysine benzoylation (Kbz). Our study identifies 22 Kbz sites on histones from HepG2 and RAW cells. This type of histone mark can be stimulated by sodium benzoate (SB), a FDA-approved drug and a widely used chemical food preservative, via generation of benzoyl CoA.

2018-07-11 | PXD010332 | Pride

SUPT3H-less SAGA coactivator can assemble and function without significantly perturbing RNA polymerase II transcription in mammalian cells

Project description:Co-activator complexes regulate chromatin accessibility and transcription. SAGA (Spt-Ada-Gcn5 Acetyltransferase) is an evolutionary conserved multisubunit co-activator complex with modular organization. The core module of SAGA constitutes the structural heart, composed of a histone octamer like structure and two additional proteins. The central histone octamer like core structure consists of six histone fold domain (HFD)-containing proteins, forming three HF pairs (TADA1/TAF12, TAF6L/TAF9/9b, and TAF10/SUPT7L) in the mammalian SAGA complexes, to which adds SUPT3H, which contains an intramolecular HF pair. The yeast homologue of SUPT3H, called Spt3, was shown to interact genetically and biochemically with the TATA binding protein (TBP). Here we investigated the role of SUPT3H in human U2OS and mouse embryonic stem (ES) cells. Using immuno-purification coupled mass spectrometry experiments we show that both human and mouse SAGA can assemble without the double HFD-containing SUPT3H. Nascent RNA-seq experiments indicted that in either U2OS or mouse ESCs lacking SUPT3H only a small subset of genes is deregulated. Consequently, in mouse ESCs SUPT3H is not essential for mouse ESC survival, but is required for ESC growth and self-renewal. In addition, TBP recruitment experiments show no major change in TBP accumulation at gene promoters in the absence of SUPT3H in mouse and human cells. Taken together our data suggest in mammalian cells SUPT3H is not required for the assembly of SAGA, general TBP recruitment to genes and cell survival, but it is important for regulating a limited set of genes.

2022-07-26 | PXD026991 | Pride

H3.1K27me1 maintains transcriptional silencing and genome stability by preventing GCN5-mediated histone acetylation

Project description:In plants, genome stability is maintained during DNA replication by the H3K27 methyltransferases ATXR5 and ATXR6, which catalyze the deposition of H3K27me1 on the replication-dependent H3.1 variant. Loss of H3.1K27me1 in atxr5 atxr6 mutants leads to heterochromatin defects, including transcriptional de-repression and genomic instability, but the molecular mechanisms involved remain largely unknown. In this study, we identified the conserved histone acetyltransferase GCN5 as a mediator of transcriptional de-repression and genomic instability in the absence of H3.1K27me1. GCN5 is part of a SAGA-like complex in plants and requires ADA2b and CHR6 to mediate the heterochromatic defects of atxr5 atxr6 mutants. Our results show that GCN5 acetylates multiple lysine residues on H3.1 variants, but that H3.1K27 and H3.1K36 play key roles in inducing genomic instability in the absence of H3.1K27me1. Overall, this work reveals a key molecular role for H3.1K27me1 in maintaining genome stability by preventing GCN5-dependent histone acetylation in plants.

2021-06-04 | GSE146126 | GEO

Genome-wide localization of Gcn5 under normal and stress conditions in S. cerevisiae and S. pombe

Project description:Here we studied genome-wide localization of Gcn5 under normal and KCl stress conditions in both yeast species. We found that in Saccharomyces cerevisiae, the enrichment of Gcn5 on genes changes from a relatively even distribution between coding region and intergenic region in the absence of stress, to a predominant localization in gene coding regions under stress conditions. This altered pattern changes are at global level indicates an important role of Gcn5 in modifying chromatin structure for stress adaptation in S. cerevisiae. The altered pattern changes are not observed in Saccharomyces pombe suggesting the different regulatory mechinery between two yeast speices. The related data series is GSE5218, where we have compared the gene regulation of Gcn5 at expression level in S. cerevisiae and S. pombe.

2010-03-01 | GSE16514 | GEO

HBO1 Catalyzes Lysine Benzoylation in Mammalian Cells

Project description:Lysine benzoylation (Kbz) is a newly discovered protein post-translational modification (PTM). This PTM can be stimulated by benzoate and contributes to gene expression. However, its regulatory enzymes and substrate proteins remain largely unknown, hindering further functional studies. Here we identified and validated the lysine acetyltransferase (KAT) HBO1 as a “writer” of Kbz in mammalian cells. In addition, we report the first benzoylome in mammalian cells, identifying 1747 Kbz sites, among them at least 77 are the HBO1-targeted Kbz substrates. Bioinformatics analysis showed that HBO1-targeted Kbz sites were involved in multiple processes, including chromatin remodeling, transcription regulation, immune regulation, and tumor growth. Our results thus identify key regulatory elements of the Kbz pathway, and reveal new enzymatic activity and functions of HBO1 in cellular physiology.

2022-10-14 | PXD034187 | Pride

Loqs-PD and R2D2 define independent pathways for RISC generation in Drosophila

Project description:In Drosophila, siRNAs are classified as endo- or exo-siRNAs based on their origin. Both are processed from double-stranded RNA precursors by Dcr-2, then loaded into the Argonaute protein Ago2. While exo-siRNAs serve to defend the cell against viruses, endo-siRNAs restrict the spread of selfish DNA in somatic cells, analogous to piRNAs in the germ line. Endo- and exo-siRNAs display a differential requirement for double-stranded RNA binding domain proteins (dsRBPs): R2D2 is needed to load exo-siRNAs into Ago2 while the PD isoform of Loquacious (Loqs-PD) stimulates Dcr-2 during the nucleolytic processing of hairpin-derived endo-siRNAs. In cell culture assays, R2D2 antagonizes Loqs-PD in endo-siRNA silencing and Loqs-PD is an inhibitor of RNA interference. Loqs-PD can interact via the C-terminus unique to this isoform with the DExH/D-helicase domain of Drosophila Dcr-2, where binding of R2D2 has also been localized. Separation of the two pathways is not complete; rather, the dicing and Ago2-loading steps appear uncoupled, analogous to the corresponding steps in miRNA biogenesis. Analysis of deep sequencing data further demonstrates that in r2d2 mutant flies, siRNAs can be loaded into Ago2 but not all siRNA classes are equally proficient for this. Thus, the canonical Ago2-RISC loading complex can be bypassed under certain circumstances. Examination of small RNAs from two different mutant strains as well as the corresponding heterozygous controls

2011-02-10 | E-GEOD-26230 | biostudies-arrayexpress

Supt3 mutant nascent RNA-seq

Project description:Coactivator complexes regulate chromatin accessibility and transcription. SAGA (Spt-Ada-Gcn5 Acetyltransferase) is an evolutionary conserved coactivator complex. The core module scaffolds the entire SAGA complex and adopts a histone octamer-like structure, which consists of six histone fold domain (HFD)-containing proteins forming three histone fold (HF) pairs, to which the double HFD-containing SUPT3H adds an HF pair. Spt3, the yeast ortholog of SUPT3H, interacts genetically and biochemically with the TATA binding protein (TBP) and contributes to global RNA polymerase II (Pol II) transcription. Here we demonstrate that i) SAGA purified from human U2OS or mouse embryonic stem cells (mESC) can assemble without SUPT3H; ii) SUPT3H is not essential for mESC survival, iii) SUPT3H is required for mESC growth and self-renewal, and iv) the loss of SUPT3H from mammalian cells affects the transcription of only a specific subset of genes. Accordingly, in the absence of SUPT3H no major change in TBP accumulation at gene promoters was observed. Thus, SUPT3H is not required for the assembly of SAGA, TBP recruitment, or overall Pol II transcription, but plays a role in mESC growth and self-renewal. Our data further suggest that yeast and mammalian SAGA complexes contribute to transcription regulation by distinct mechanisms.

2022-07-07 | GSE202823 | GEO

Kinetics of Enzymatic Mercury Methylation at Nanomolar Concentrations Catalyzed by HgcAB.

Project description: Not available

| S-EPMC6581168 | biostudies-literature

Fronts and pulses in an enzymatic reaction catalyzed by glucose oxidase.

Project description: Not available

| S-EPMC1855356 | biostudies-literature

Transcription profiling of Arabidopsis gcn5 knockout mutants

Project description:Two gcn5 KO mutants were grown on MS during 10 days (1.03 boyes stage) : gcn5-1 and gcn5-2. Each mutant was compared to the wild type (Ws)

2008-02-07 | E-MEXP-1241 | biostudies-arrayexpress

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