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Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

ABSTRACT: Basis of Specificity for a Conserved Promiscuous Chromatin Remodeling Protein

PROVIDER: PRJNA630194 | 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

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

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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

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