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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2 [RNA-Seq]

ABSTRACT: Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2 [RNA-Seq]

PROVIDER: PRJNA735739 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14750867.fastq.gz	Fastqsanger.gz
	SRR14750868.fastq.gz	Fastqsanger.gz
	SRR14750869.fastq.gz	Fastqsanger.gz
	SRR14750870.fastq.gz	Fastqsanger.gz
	SRR14750871.fastq.gz	Fastqsanger.gz

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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2

Project description:Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2

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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2 [ChIP-Seq]

Project description:Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2 [ChIP-Seq]

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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2 [ChIP-Seq]

Project description:Ribosome biogenesis is an essential cellular process that requires integration of extracellular cues, such as metabolic state, with intracellular signaling, transcriptional regulation and chromatin accessibility at the ribosomal DNA. Here, we demonstrate that the recently identified histone modification, methylation of H2AQ105, is an integral part of a dynamic chromatin network at the rDNA locus. Its deposition depends on a functional mTor signaling pathway as well as acetylation of histone H3 at position K56, thus integrating signals from cell cycle, metabolic and proliferative states. Furthermore, we identify a first epigenetic reader of this modification, the ribonucleoprotein Nhp2, which specifically recognizes the methylation on H2AQ105. Based on functional and proteomic data we suggest that Nhp2 functions as an adapter to bridge the rDNA chromatin with components of the small subunit processome to efficiently coordinate transcription of rRNA with its post-transcriptional processing. We support this by showing that an H2AQ105A mutant has a mild defect in early processing of the rRNA.

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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2 [RNA-Seq]

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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2

Project description:Ribosome biogenesis is an essential process within cells that requires integration of extracellular cues such as metabolic states through signaling with transcriptional regulation and maintenance of accessible chromatin at the ribosomal DNA. Here, we demonstrate that the recently identified histone modification, methylation of H2AQ105 is an integral part of a dynamic chromatin network at the rDNA locus. Its deposition depends on a functional mTor signaling pathway and acetylation of histone H3 at position K56, thus integrating signals from cell cycle and proliferative states. Furthermore, we identify a first epigenetic reader of this modification. The ribonucleoprotein Nhp2 specifically recognizes methylation H2AQ105me. Based on functional and proteomic data we suggest that Nhp2 functions as an adapter to bridge chromatin and components of the small subunit processome and might help to efficiently coordinate transcription of rRNA with its post-transcriptional processing.

2021-08-06 | PXD023510 | Pride

Fbxl10 regulates PRC1 recruitment to CpG islands and H2A ubiquitination

Project description:Polycomb repressive complex 1 (PRC1) catalyzes H2A monoubiquitination (uH2A) and regulates pluripotency in embryonic stem cells (ESCs). However the mechanisms controlling PRC1 recruitment and activity are largely unknown. Here we show that Fbxl10 interacts with Ring1B and Nspc1, forming a non-canonical PRC1. We demonstrate that Fbxl10-PRC1 is essential for H2A ubiquitination in mouse ESCs. Genome-wide analyses reveal that Fbxl10 preferentially binds to CpG islands and co-localizes with Ring1B on Polycomb target genes. Notably, Fbxl10 depletion causes modest dissociation of Ring1B but a major loss of uH2A on target genes. Furthermore rescue experiments for Fbxl10 reveal that its DNA binding capability and integration into PRC1 are required for proper H2A ubiquitination. ES cells lacking Fbxl10, like previously characterized Polycomb mutants, show a severely compromised capacity for successful differentiation. Our results shed light on a novel mechanism how CpG islands regulate chromatin function by affecting polycomb recruitment and activity. All ChIP-seq reactions were performed in either untransfected cells, cells expressing scrambled shRNA or Fbxl10 shRNA, Ring1b-/- or Suz12-/- mouse ES cells

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Methylation of Q105 on histone H2A is part of a dynamic regulatory mechanism integrating metabolism with ribosome biogenesis through recruitment of Nhp2

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Fbxl10 regulates PRC1 recruitment to CpG islands and H2A ubiquitination

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