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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast

ABSTRACT: Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast

PROVIDER: PRJNA498393 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8109500_1.fastq.gz	Fastqsanger.gz
	SRR8109500_2.fastq.gz	Fastqsanger.gz
	SRR8109510_1.fastq.gz	Fastqsanger.gz
	SRR8109510_2.fastq.gz	Fastqsanger.gz
	SRR8109520_1.fastq.gz	Fastqsanger.gz

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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast (ChIP-seq)

Project description:Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast (ChIP-seq)

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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast (RNA-seq)

Project description:Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast (RNA-seq)

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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast.

Project description:In yeast, Hda1 histone deacetylase complex (Hda1C) preferentially deacetylates histones H3 and H2B, and functionally interacts with Tup1 to repress transcription. However, previous studies identified global increases in histone H4 acetylation in cells lacking Hda1, a component of Hda1C. Here, we find that Hda1C binds to hyperactive genes, likely via the interaction between the Arb2 domain of Hda1 and RNA polymerase II. Additionally, we report that Hda1C specifically deacetylates H4, but not H3, at hyperactive genes to partially inhibit elongation. This role is contrast to that of the Set2-Rpd3S pathway deacetylating histones at infrequently transcribed genes. We also find that Hda1C deacetylates H3 at inactive genes to delay the kinetics of gene induction. Therefore, in addition to fine-tuning of transcriptional response via H3-specific deacetylation, Hda1C may modulate elongation by specifically deacetylating H4 at highly transcribed regions.

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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast (RNA-seq)

Project description:Hda1C directly binds to actively transcribed regions likely via the interaction with elongating RNA PolII and/or with nascent RNA transcripts. The Arb2 domain of Hda1 is also critical for its binding to chromatin. Interestingly, Hda1C specifically deacetylates histone H4 but not H3 at active genes to suppress nucleosome instability and partially inhibit elongation. In contrast, Hda1C mainly deacetylates histone H3 at inactive genes to delay gene induction.

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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast (ChIP-seq)

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Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast

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

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Project description:Histone acetylation and deacetylation are among the principal mechanisms by which chromatin is regulated during transcription, DNA silencing, and DNA repair. We analyzed patterns of genetic interactions uncovered during comprehensive genome-wide analyses in yeast to probe how histone acetyltransferase (HAT) and histone deacetylase (HDAC) protein complexes interact. The genetic interaction data unveil an underappreciated role of HDACs in maintaining cellular viability, and led us to show that deacetylation of the histone variant Htz1p at lysine 14 is mediated by Hda1p. Studies of the essential nucleosome acetyltransferase of H4 (NuA4) revealed acetylation-dependent protein stabilization of Yng2p, a potential nonhistone substrate of NuA4 and Rpd3C, and led to a new functional organization model for this critical complex. We also found that DNA double-stranded breaks (DSBs) result in local recruitment of the NuA4 complex, followed by an elaborate NuA4 remodeling process concomitant with Rpd3p recruitment and histone deacetylation. These new characterizations of the HDA and NuA4 complexes demonstrate how systematic analyses of genetic interactions may help illuminate the mechanisms of intricate cellular processes. Keywords: genetic modification

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