Dido3 PHD Modulates Cell Differentiation and Division

被引：48

作者：

Gatchalian, Jovylyn ^{[1
]}

Fuetterer, Agnes ^{[2
]}

Rothbart, Scott B. ^{[3
,4
]}

Tong, Qiong ^{[1
]}

Rincon-Arano, Hector ^{[5
]}

Sanchez de Diego, Ainhoa ^{[2
]}

Groudine, Mark ^{[5
,6
]}

Strahl, Brian D. ^{[3
,4
]}

Martinez-A, Carlos ^{[2
]}

van Wely, Karel H. M. ^{[2
]}

Kutateladze, Tatiana G. ^{[1
]}

机构：

[1] Univ Colorado, Sch Med, Dept Pharmacol, Aurora, CO 80045 USA

[2] CSIC, Ctr Nacl Biotecnol, Dept Immunol & Oncol, E-28049 Madrid, Spain

[3] Univ N Carolina, Sch Med, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA

[4] Univ N Carolina, Sch Med, Lineberger Comprehens Canc Ctr, Chapel Hill, NC 27599 USA

[5] Fred Hutchinson Canc Res Ctr, Div Basic Sci, Seattle, WA 98109 USA

[6] Univ Washington, Sch Med, Dept Radiat Oncol, Seattle, WA 98195 USA

来源：

CELL REPORTS | 2013年 / 4卷 / 01期

基金：

美国国家卫生研究院;

关键词：

HISTONE H3; PLANT HOMEODOMAIN; IN-VITRO; PHOSPHORYLATION; RECOGNITION; GENE;

D O I：

10.1016/j.celrep.2013.06.014

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Death Inducer Obliterator 3 (Dido3) is implicated in the maintenance of stem cell genomic stability and tumorigenesis. Here, we show that Dido3 regulates the expression of stemness genes in embryonic stem cells through its plant homeodomain (PHD) finger. Binding of Dido3 PHD to histone H3K4me3 is disrupted by threonine phosphorylation that triggers Dido3 translocation from chromatin to the mitotic spindle. The crystal structure of Dido3 PHD in complex with H3K4me3 reveals an atypical aromatic-cage-like binding site that contains a histidine residue. Biochemical, structural, and mutational analyses of the binding mechanism identified the determinants of specificity and affinity and explained the inability of homologous PHF3 to bind H3K4me3. Together, our findings reveal a link between the transcriptional control in embryonic development and regulation of cell division.

引用

页码：148 / 158

页数：11

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