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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [RNA-Seq]

ABSTRACT: Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [RNA-Seq]

PROVIDER: PRJNA630199 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11684203_1.fastq.gz	Fastqsanger.gz
	SRR11684203_2.fastq.gz	Fastqsanger.gz
	SRR11684204_1.fastq.gz	Fastqsanger.gz
	SRR11684204_2.fastq.gz	Fastqsanger.gz
	SRR11684205_1.fastq.gz	Fastqsanger.gz

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

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Basis of specificity for a conserved and promiscuous chromatin remodeling protein.

Project description:Eukaryotic genomes are organized dynamically through the repositioning of nucleosomes. Isw2 is an enzyme that has been previously defined as a genome-wide, nonspecific nucleosome spacing factor. Here, we show that Isw2 instead acts as an obligately targeted nucleosome remodeler in vivo through physical interactions with sequence-specific factors. We demonstrate that Isw2-recruiting factors use small and previously uncharacterized epitopes, which direct Isw2 activity through highly conserved acidic residues in the Isw2 accessory protein Itc1. This interaction orients Isw2 on target nucleosomes, allowing for precise nucleosome positioning at targeted loci. Finally, we show that these critical acidic residues have been lost in the Drosophila lineage, potentially explaining the inconsistently characterized function of Isw2-like proteins. Altogether, these data suggest an 'interacting barrier model,' where Isw2 interacts with a sequence-specific factor to accurately and reproducibly position a single, targeted nucleosome to define the precise border of phased chromatin arrays.

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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

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

2020-08-31 | GSE149804 | GEO

Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [RNA-Seq]

Project description:We propose an interacting barrier mechanism for cooperation between Isw2-related proteins and sequence-specific DNA binding factors.

2020-08-31 | GSE149803 | GEO

Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [ChIP-Seq]

Project description:We propose an interacting barrier mechanism for cooperation between Isw2-related proteins and sequence-specific DNA binding factors.

2020-08-31 | GSE149801 | GEO

Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein [Mnase-seq]

Project description:We propose an interacting barrier mechanism for cooperation between Isw2-related proteins and sequence-specific DNA binding factors.

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A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme

Project description:The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange where either H2A.Z or H2A can be exchanged from nucleosomes. This result is confirmed in vivo, where genome-wide analysis demonstrates widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a M-bM-^@M-^\lockM-bM-^@M-^] that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators. H2A.Z ChIP seq experiments in mutants with constitutive H3K56ac

2013-04-15 | E-GEOD-43935 | biostudies-arrayexpress

A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme

Project description:The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange where either H2A.Z or H2A can be exchanged from nucleosomes. This result is confirmed in vivo, where genome-wide analysis demonstrates widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a “lock” that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators.

2013-04-15 | GSE43935 | GEO

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