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RTF1 mediates epigenetic control of Th17 cell differentiation via H2B monoubiquitination [RNA-seq]

ABSTRACT: RTF1 mediates epigenetic control of Th17 cell differentiation via H2B monoubiquitination [RNA-seq]

PROVIDER: PRJNA1121921 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29339266_1.fastq.gz	Fastqsanger.gz
	SRR29339266_2.fastq.gz	Fastqsanger.gz
	SRR29339267_1.fastq.gz	Fastqsanger.gz
	SRR29339267_2.fastq.gz	Fastqsanger.gz
	SRR29339268_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

RTF1 mediates epigenetic control of Th17 cell differentiation via H2B monoubiquitination [CUT&RUN]

Project description:The transcription factor RTF1 has been identified as a gene associated with an increased risk of ulcerative colitis (UC) . In this study, we investigated its impact on modulating intestinal inflammation through the control of T cells expressing interleukin-17A (Th17) cells. Our results demonstrate that RTF1 deficiency disrupts the differentiation of Th17 cells, while leaving regulatory T cells (Treg) cells unaffected. Mechanistically, RTF1 facilitates Histone H2B monoubiquitination (H2Bub1), which requires its histone modification domain (HMD). Impaired Th17 differentiation was also observed in cells lacking the H2Bub1 E3 ligase subunit RNF40. This study underscores the essential role of RTF1 in H2Bub1-mediated epigenetic regulation of Th17 cell differentiation. Understanding this process provides valuable insight into addressing Th17-associated inflammatory disorders.

2025-04-03 | GSE269642 | GEO

RTF1 mediates epigenetic control of Th17 cell differentiation via H2B monoubiquitination [RNA-seq]

2025-04-03 | GSE269436 | GEO

RTF1 mediates epigenetic control of Th17 cell differentiation via H2B monoubiquitination [CUT&RUN]

Project description:RTF1 mediates epigenetic control of Th17 cell differentiation via H2B monoubiquitination [CUT&RUN]

| PRJNA1122923 | ENA

Rtf1 HMD domain facilitates global histone H2B monoubiquitination and regulates morphogenesis and virulence in the meningitis-causing pathogen Cryptococcus neoformans

Project description:Rtf1 is generally considered to be a subunit of the Paf1 complex (Paf1C), which is a multifunctional protein complex involved in histone modification and RNA biosynthesis at multiple stages. Rtf1 is stably associated with the Paf1C in Saccharomyces cerevisiae, but not in other species including humans. Little is known about its function in human fungal pathogens. Here, we show that Rtf1 is required for facilitating H2B monoubiquitination (H2Bub1), and regulates fungal morphogenesis and pathogenicity in the meningitis-causing fungal pathogen Cryptococcus neoformans. Rtf1 is not tightly associated with the Paf1C, and its histone modification domain (HMD) is sufficient to promote H2Bub1 and the expression of genes related to fungal mating and filamentation. Moreover, Rtf1 HMD fully restores fungal morphogenesis and pathogenicity; however, it fails to restore defects of thermal tolerance and melanin production in the rtf1Δ strain background. The present study establishes a role for cryptococcal Rtf1 as a Paf1C-independent regulator in regulating fungal morphogenesis and pathogenicity, and highlights the function of HMD in facilitating global H2Bub1 in C. neoformans.

2025-05-05 | GSE296031 | GEO

GlcNAcylation of histone H2B facilitates its monoubiquitination

Project description:This SuperSeries is composed of the following subset Series: GSE33049: GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data] GSE33050: GlcNAcylation of histone H2B facilitates its monoubiquitination [Affymetrix data] Refer to individual Series

2011-10-26 | E-GEOD-33051 | biostudies-arrayexpress

GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

Project description:We report that histone GlcNAcylation of H2B S112 is a vital histone modification which facilitates histone monoubiquitination (ub). In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over entire chromosomes including transcribed gene loci, together with co-localization of H2B S112 GlcNAcylation and K120 ub. Examination of H2B S112 GlcNAc and H2B K120 ub in HeLa S3 cells

2011-10-27 | E-GEOD-33049 | biostudies-arrayexpress

GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

2011-10-27 | GSE33049 | GEO

Co-dependency of H2B monoubiquitination and nucleosome re-assembly on Chd1

Project description:Monoubiquitination of histone H2B on lysine 123 (H2BK123ub) is a transient histone modification considered to be essential for establishing H3K4 and H3K79 trimethylation by Set1/COMPASS and Dot1, respectively. Many of the factors such as Rad6/Bre1, the Paf1 complex, and the Bur1/Bur2 complex were identified to be required for proper histone H3K4 and H3K79 trimethylation, and were shown to function by regulating H2BK123ub levels. Here, we have identified Chd1 as a factor that is required for proper maintenance of H2B monoubiquitination levels, but not for H3K4 and H3K79 trimethylation. Loss of Chd1 results in a substantial loss of H2BK123ub levels with little to no effect on the genome-wide pattern of H3K4 and H3K79 trimethylation. Our data shows that nucleosomal occupancy is reduced in gene bodies in both CHD1 null and K123A backgrounds. We have also demonstrated that Chd1’s function in maintaining H2BK123ub levels is conserved from yeast to human. Our study provides evidence that only small levels of H2BK123ub are necessary for full levels of H3K4 and H3K79 trimethylation in vivo, and points to a role for Chd1 in positively regulating gene expression through promoting nucleosome re-assembly coupled with H2B monoubiquitination. Examination of two histone modifications in wild-type and Chd1 null yeast strains using ChIP-seq. Expression profiling in wild-type and Chd1 null yeast strains using RNA-seq.

2012-05-01 | E-GEOD-36334 | biostudies-arrayexpress

Co-dependency of H2B monoubiquitination and nucleosome re-assembly on Chd1

2012-05-02 | GSE36334 | GEO

The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Promotes H2B Ubiquitylation Through a Direct Interaction with the Ubiquitin Conjugase Rad6

Project description:Transcription by RNA polymerase II is regulated by epigenetic modifications to the chromatin template. The mono-ubiquitylation of H2B is established during transcription elongation and broadly impacts chromatin architecture and gene expression. The Polymerase Associated Factor 1 complex (Paf1C) is required for H2B ubiquitylation through an unknown mechanism. Here, we find that a 66-amino acid histone modification domain (HMD) within the Rtf1 subunit of Paf1C promotes H2B ubiquitylation in cells lacking all Paf1C members and present the crystal structure of this domain. Using site-specific in vivo crosslinking, we show that Rtf1 directly interacts with the ubiquitin conjugase Rad6 through a conserved surface on the HMD. Through ChIP-exo analysis, we observe that enrichment of Paf1C correlates with H2B ubiquitylation, and that the HMD, Rad6 and Bre1 localize to H2B. Finally, we demonstrate that the HMD directly stimulates H2B ubiquitylation in a reconstituted system, arguing that Paf1C functions as a cofactor for Rad6-Bre1 mediated catalysis.

2016-11-07 | GSE83348 | GEO

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