Protein & Cell >

2017 , Vol. 8 >Issue 10: 767 - 771

DOI: https://doi.org/10.1007/s13238-017-0462-y

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Structural basis for DAXX interaction with ATRX

  • Xiaoman Wang 1 ,
  • Yiyue Zhao 1,2 ,
  • Jian Zhang 1 ,
  • Yong Chen , 1,2
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  • 1. State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 201210, China
  • 2. School of Life Science and Technology, Shanghai Tech University, Shanghai 201210, China

Published date: 06 Nov 2017

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2017 The Author(s) 2017. This article is an open access publication
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Cite this article

Xiaoman Wang , Yiyue Zhao , Jian Zhang , Yong Chen . Structural basis for DAXX interaction with ATRX[J]. Protein & Cell, 2017 , 8(10) : 767 -771 . DOI: 10.1007/s13238-017-0462-y

References

Publishing order | Descend order by publishing year | Descend order by cited within
1
ClynesD, HiggsDR, GibbonsRJ (2013) The chromatin remodeller ATRX: a repeat offender in human disease. Trends Biochem Sci38:461–466

DOI

2
DyerMA, Qadeer, Z.A., Valle-Garcia,D., and BernsteinE (2017) ATRX and DAXX: Mechanisms and Mutations. Cold Spring Harb Perspect Med7.

DOI

3
ElsasserSJ, HuangH, LewisPW, ChinJW, AllisCD, PatelDJ (2012) DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature491:560–565

DOI

4
Escobar-CabreraE, LauDK, GiovinazziS, IshovAM, McIntoshLP (2010) Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. Structure18:1642–1653

DOI

5
GoldbergAD, BanaszynskiLA, NohKM, LewisPW, ElsaesserSJ, StadlerS, DewellS, LawM, GuoX, LiX (2010) Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell140:678–691

DOI

6
GostissaM, MorelliM, MantovaniF, GuidaE, PiazzaS, CollavinL, BrancoliniC, SchneiderC, Del SalG (2004) The transcriptional repressor hDaxx potentiates p53-dependent apoptosis. J Biol Chem279:48013–48023

DOI

7
IwaseS, XiangB, GhoshS, RenT, LewisPW, CochraneJC, AllisCD, PickettsDJ, PatelDJ, LiH (2011) ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome. Nat Struct Mol Biol18:769–776

DOI

8
LawMJ, LowerKM, VoonHP, HughesJR, GarrickD, ViprakasitV, MitsonM, De GobbiM, MarraM, MorrisA (2010) ATR-X syndrome protein targets tandem repeats and influences allelespecific expression in a size-dependent manner. Cell143:367–378

DOI

9
LewisPW, ElsaesserSJ, NohKM, StadlerSC, AllisCD (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc Natl Acad Sci USA107:14075–14080

DOI

10
LindsayCR, MorozovVM, IshovAM (2008) PML NBs (ND10) and Daxx: from nuclear structure to protein function. Front Biosci13:7132–7142

DOI

11
LiuCP, XiongC, WangM, YuZ, YangN, ChenP, ZhangZ, LiG, XuRM (2012) Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX. Nat Struct Mol Biol19:1287–1292

DOI

12
TangJ, WuS, LiuH, StrattR, BarakOG, ShiekhattarR, PickettsDJ, YangX (2004) A novel transcription regulatory complex containing death domain-associated protein and the ATR-X syndrome protein. J Biol Chem279:20369–20377

DOI

13
TangJ, QuLK, ZhangJ, WangW, MichaelsonJS, DegenhardtYY, El-DeiryWS, YangX (2006) Critical role for Daxx in regulating Mdm2. Nat Cell Biol8:855–862

DOI

14
WatsonLA, GoldbergH, BerubeNG (2015) Emerging roles of ATRX in cancer. Epigenomics7:1365–1378

DOI

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