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Potential Functions of Histone H3.3K56 Acetylation in Mammals

ABSTRACT: To decipher the functions of histone H3.3 acetylation at lysine 56 in mammals using a cellular system.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Lei Fang

LAB HEAD: Lei Fang

PROVIDER: PXD022580 | Pride | 2022-06-09

REPOSITORIES: Pride

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			Action	DRS
	20161010-01.wiff	Wiff
	20161010-01.wiff.scan	Wiff
	20161010-02.wiff	Wiff
	20161010-02.wiff.scan	Wiff
	20161010-03.wiff	Wiff

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Publications

Potential functions of histone H3.3 lysine 56 acetylation in mammals.

Fang Lei L Chen Danqi D Zhang Jingzi J Li Hongjie H Bradford Beatrix B Jin Chunyuan C

Epigenetics 20210524 5

H3K56 acetylation (H3K56Ac) was first identified in yeast and has recently been reported to play important roles in maintaining genomic stability, chromatin assembly, DNA replication, cell cycle progression and DNA repair. Although H3.1K56Ac has been relatively well studied, the function of H3.3K56Ac remains mostly unknown in mammals. In this study, we used H3.3K56Q and H3.3K56R mutants to study the possible function of H3.3K56 acetylation. The K-to-Q substitution mimics a constitutively acetyla ...[more]

PMID: 33902396

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Potential functions of histone H3.3 lysine 56 acetylation in mammals.

Project description:H3K56 acetylation (H3K56Ac) was first identified in yeast and has recently been reported to play important roles in maintaining genomic stability, chromatin assembly, DNA replication, cell cycle progression and DNA repair. Although H3.1K56Ac has been relatively well studied, the function of H3.3K56Ac remains mostly unknown in mammals. In this study, we used H3.3K56Q and H3.3K56R mutants to study the possible function of H3.3K56 acetylation. The K-to-Q substitution mimics a constitutively acetylated lysine, while the K-to-R replacement mimics a constitutively unmodified lysine. We report that cell lines harbouring mutation of H3.3K56R exhibit increased cell death and dramatic morphology changes. Using a Tet-Off inducible system, we found an increased population of polyploid/aneuploid cells and decreased cell viability in H3.3K56R mutant cells. Consistent with these results, the H3.3K56R mutant had compromised H3.3 incorporation into several pericentric and centric heterochromatin regions we tested. Moreover, mass spectrometry analysis coupled with label-free quantification revealed that biological processes regulated by the H3.3-associating proteins, whose interaction with H3.3 was markedly increased by H3.3K56Q mutation but decreased by H3.3K56R mutation, include sister chromatid cohesion, mitotic nuclear division, and mitotic nuclear envelope disassembly. These results suggest that H3.3K56 acetylation is crucial for chromosome segregation and cell division in mammals.

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