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IlLycPorp

ABSTRACT: Lycophotia porphyrea (true lover's knot)

PROVIDER: PRJEB61365 | ENA |

REPOSITORIES: ENA

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Dataset's files

Source:

			Action	DRS
		Other
	ERR11242142.fastq.gz	Fastqsanger.gz
	ERR11242566_1.fastq.gz	Fastqsanger.gz
	ERR11242566_2.fastq.gz	Fastqsanger.gz
	ERR12035189_1.fastq.gz	Fastqsanger.gz

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Project description:KAT8 is a lysine acetyltransferase and is involved in multiple important biological processes including cancer. The well-known function of KAT8 is catalyzing acetylation on histone H4, which regulates gene expression and chromatin decompaction. Besides catalytic HAT domain, the function of Tudor-knot domain of KAT8 remains largely unclear. Here, we report a novel function of Tudor-knot domain in facilitates histone acetyltransferase activity on H4K16ac. One hot-spot cancer mutation on Tudor-knot domain of KAT8 inhibits its interaction with nucleosome and reduces H4K16ac level both in vitro and in cells without altering the chromatin occupancy. Interestingly, this Tudor-knot mutation does not influence acetylation activity of KAT8 on p53, a non-histone substrate, suggests the important function of KAT8 Tudor-knot domain in the substrate specific catalytic regulation.

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