Protein & Cell >

2017 , Vol. 8 >Issue 10: 762 - 766

DOI: https://doi.org/10.1007/s13238-017-0463-x

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Structural and biochemical characterization of DAXX-ATRX interaction

  • Zhuang Li 1,2 ,
  • Dan Zhao 2 ,
  • Bin Xiang 1 ,
  • Haitao Li , 2
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  • 1. College of Life Sciences, Peking University, Beijing 100871, China
  • 2. MOE Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing 100084, 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

Zhuang Li , Dan Zhao , Bin Xiang , Haitao Li . Structural and biochemical characterization of DAXX-ATRX interaction[J]. Protein & Cell, 2017 , 8(10) : 762 -766 . DOI: 10.1007/s13238-017-0463-x

References

Publishing order | Descend order by publishing year | Descend order by cited within
1
DraneP, OuararhniK, DepauxA, ShuaibM, HamicheA (2010) The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3.Genes Dev24:1253–1265

DOI

2
ElsasserSJ, HuangH, LewisPW, ChinJW, AllisCD, PatelDJ (2012) DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition.Nature491:560–565

DOI

3
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

4
GibbonsRJ, PickettsDJ, VillardL, HiggsDR (1995) Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome).Cell80:837–845

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
HeQ, KimH, HuangR, LuW, TangM, ShiF, YangD, ZhangX, HuangJ, LiuD (2015) The Daxx/Atrx complex protects tandem repetitive elements during DNA hypomethylation by promoting H3K9 trimethylation.Cell Stem Cell17:273–286

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
KimEJ, ParkJS, UmSJ (2003) Identification of Daxx interacting with p73, one of the p53 family, and its regulation of p53 activity by competitive interaction with PML.Nucleic Acids Res31:5356–5367

DOI

9
KitagawaD, KajihoH, NegishiT, UraS, WatanabeT, WadaT, IchijoH, KatadaT, NishinaH (2006) Release of RASSF1C from the nucleus by Daxx degradation links DNA damage and SAPK/JNK activation.EMBO J25:3286–3297

DOI

10
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

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
NohKM, MazeI, ZhaoD, XiangB, WenderskiW, LewisPW, ShenL, LiH, AllisCD (2015) ATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neurons.Proc Natl Acad Sci USA112:6820–6827

DOI

13
RatnakumarK, BernsteinE (2013) ATRX: the case of a peculiar chromatin remodeler.Epigenetics8:3–9

DOI

14
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

15
TangJ, QuLK, ZhangJ, WangW, MichaelsonJS, DegenhardtYY, El-DeiryWS, YangX (2006) Critical role for Daxx in regulating Mdm2.Nat Cell Biol8:855–862

DOI

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