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Lysine Catabolism Reprograms Tumour Immunity through Histone Crotonylation.

ABSTRACT: Lysine Catabolism Reprograms Tumour Immunity through Histone Crotonylation.

PROVIDER: PRJNA860225 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR20323906_1.fastq.gz	Fastqsanger.gz
	SRR20323906_2.fastq.gz	Fastqsanger.gz
	SRR20323907_1.fastq.gz	Fastqsanger.gz
	SRR20323907_2.fastq.gz	Fastqsanger.gz
	SRR20323908_1.fastq.gz	Fastqsanger.gz

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Lysine Degradation Reprograms Tumour Immunity through Histone Crotonylation [ChIP-seq]

Project description:Lysine Degradation Reprograms Tumour Immunity through Histone Crotonylation [ChIP-seq]

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Lysine Degradation Reprograms Tumour Immunity through Histone Crotonylation [RNA-seq]

Project description:Lysine Degradation Reprograms Tumour Immunity through Histone Crotonylation [RNA-seq]

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Lysine Degradation Reprograms Tumour Immunity through Histone Crotonylation [ChIP-seq]

Project description:To understand how GCDH enhances the oncogenic traits in GSCs, we carried out comparative transcriptomic analysis in two patient-derived GSCs (GSC23, GSC3028) with or without GCDH depletion to identify the driving events. To further examine the connection between lysine catabolism and GSC functions, we controlled L-lysine culture concentrations (0.2 and 2 mM) of GSCs in lysine-deprived media and performed RNA-seq. To address the functional significance of ECHS1 loss in tumour biology, we carried out RNA-seq in two early-passage DGCs (DGC23, DGC3028) with or without ECHS1 depletion. Kcr, H3K27ac or H3K9me3 ChIP-seq was performed in GSC23 to understand the molecular basis of how GCDH loss or lysine restriction affects chromatin landscape.

2023-03-16 | GSE208617 | GEO

Lysine Degradation Reprograms Tumour Immunity through Histone Crotonylation [RNA-seq]

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Lysine Catabolism Reprograms Tumour Immunity through Histone Crotonylation.

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-03-15 | GSE208618 | GEO

Histone Lysine Crotonylation Regulates Long-Term Memory Storage

Project description:Utilizing a single nuclei multiomics approach, this study elucidates how enhancing histone lysine crotonylation regulates cell type specific gene expression and chromatin accessibility during memory consolidation.

2024-11-13 | GSE281007 | GEO

Large-scale identification of lysine crotonylation

Project description:Lysine crotonylation on histones is a recently identified post-translational modification that has been demonstrated to associate with active promoters and to directly stimulate transcription.Given that crotonyl-CoA is essential for the acyl transfer reaction and it is a metabolic intermediate widely localized within the cell, we postulate that lysine crotonylation on non-histone proteins could also widely exist. Using specific antibody to enrich crotonylated lysine(Kcr) peptides followed by high-resolution mass spectrometry analysis reveals that crotonylated proteins and lysine residues. Bioinformatic analysis reveals that crotonylated proteins are particularly enriched in the nuclei, that lysine crotonylation alters level of the modified proteins in the chromatin and that cotonylation of a subset of proteins influences DNA replication and cell cycle. Taken together, our data indicate that lysine crotonylation could be induced in a large number of proteins other than histones and this type of acyl modification could play an important role regulating multiple cellular processes.

2016-06-11 | MSV000079810 | MassIVE

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

Histone Lysine Crotonylation Regulates Long-Term Memory Storage

Project description:Histone Lysine Crotonylation Regulates Long-Term Memory Storage

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Qualitative Proteome-wide Analysis Reveal the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense C. Z. Tang et S. J. Cheng

Project description:Lysine crotonylation of histone proteins is a newly identified post-translational modification with diversified cellular functions. However, there’s few reports on lysine crotonylation of non-histone proteins in fruit plant cells. By using high-resolution LC-MS coupled with highly sensitive specific immune-affinity antibody analysis, a whole crotonylation proteome analysis of Dendrobium huoshanese was performed. In total, 1,591 proteins with 4,725 lysine crotonylation sites were found, among them eleven conserved motifs have been identified. Bioinformatic analysis linked crotonylated proteins to multiple metabolic pathways, including secondary metabolites biosynthesis, transport and catabolism; energy production and conversion; carbohydrate transport and metabolism; and translation, ribosomal structure and biogenesis.

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