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ASH-1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin

ABSTRACT: ASH-1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin

PROVIDER: PRJNA485801 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7690280.fastq.gz	Fastqsanger.gz
	SRR7690290.fastq.gz	Fastqsanger.gz
	SRR7690271.fastq.gz	Fastqsanger.gz
	SRR7690281.fastq.gz	Fastqsanger.gz
	SRR7690272.fastq.gz	Fastqsanger.gz

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ASH-1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin

Project description:ASH-1 orthologs are H3K36-specific methyltransferases that are conserved from fungi to humans but are poorly understood, in part because they are typically essential for viability. Here we examine the H3K36 methylation pathway of Neurospora crassa, which we find has just two H3K36 methyltransferases, ASH-1 and RNA polymerase II-associated SET-2. Our investigation of the interplay between SET-2 and ASH-1 uncovered a regulatory mechanism connecting ASH-1-catalyzed H3K36 methylation to repression of poorly transcribed genes. Our findings provide new insight into ASH-1 function, H3K27me2/3 establishment, and repression at facultative heterochromatin.

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ASH1-catalyzed H3K36 methylation drives gene repression and marks H3K27me2/3-competent chromatin.

Project description:Methylation of histone H3 at lysine 36 (H3K36me), a widely-distributed chromatin mark, largely results from association of the lysine methyltransferase (KMT) SET-2 with RNA polymerase II (RNAPII), but most eukaryotes also have additional H3K36me KMTs that act independently of RNAPII. These include the orthologs of ASH1, which are conserved in animals, plants, and fungi but whose function and control are poorly understood. We found that Neurospora crassa has just two H3K36 KMTs, ASH1 and SET-2, and were able to explore the function and distribution of each enzyme independently. While H3K36me deposited by SET-2 marks active genes, inactive genes are modified by ASH1 and its activity is critical for their repression. ASH1-marked chromatin can be further modified by methylation of H3K27, and ASH1 catalytic activity modulates the accumulation of H3K27me2/3 both positively and negatively. These findings provide new insight into ASH1 function, H3K27me2/3 establishment, and repression in facultative heterochromatin.

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