A chromodomain switch mediated by histone H3 Lys 4 acetylation regulates heterochromatin assembly

被引：72

作者：

Xhemalce, Blerta ^{[1
]}

Kouzarides, Tony ^{[1
]}

机构：

[1] Univ Cambridge, Wellcome Trust Canc Res UK Gurdon Inst, Cambridge CB2 1QN, England

来源：

GENES & DEVELOPMENT | 2010年 / 24卷 / 07期

关键词：

H3K4ac; HP1; RITS complex; chromodomain switch; heterochromatin; FISSION YEAST; LYSINE-9; METHYLATION; HP1; PROTEINS; MAINTENANCE; RITS; DNA; METHYLTRANSFERASE; RECRUITMENT; CENTROMERE; COMPLEXES;

D O I：

10.1101/gad.1881710

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Chromodomain proteins (Chp1/Chp2/Swi6/Clr4) bind to methylated H3K9 (H3K9me) and regulate pericentric heterochromatin in fission yeast. Chp1 and Clr4 (H3K9-HMT), bind transcriptionally active heterochromatin, whereas Chp2/Swi6 (HP1 homologs) are recruited during the inactive state. We show that H3K4 acetylation (H3K4ac) plays a role in the transition of dimethylated H3K9 (H3K9me2) occupancy from Chp1/Clr4 to Chp2/Swi6. H3K4ac, mediated by Mst1, is enriched at pericentromeres concomitantly with heterochromatin reassembly. H3K4R (Lys --> Arg) mutation increases Chp1 and decreases Chp2/Swi6 pericentric occupancy and exhibits centromeric desilencing. Consistent with structural data, H3K4ac specifically reduces Chp1/Clr4 affinity to H3K9me. We propose that H3K4ac mediates a chromodomain switch from Chp1/Clr4 to Swi6/Chp2 to allow heterochromatin reassembly.

引用

页码：647 / 652

页数：6

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