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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

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

PROVIDER: PRJNA735734 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14750600.fastq.gz	Fastqsanger.gz
	SRR14750601.fastq.gz	Fastqsanger.gz
	SRR14750867.fastq.gz	Fastqsanger.gz
	SRR14750868.fastq.gz	Fastqsanger.gz
	SRR14750869.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 [RNA-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 [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 [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 [RNA-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 [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

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.

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Fbxl10 regulates PRC1 recruitment to CpG islands and H2A ubiquitination

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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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