Structural basis underlying viral hijacking of a histone chaperone complex.
Structural basis underlying viral hijacking of a histone chaperone complex.
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DOI：
10.1038/ncomms12707
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发表时间：
2016-09-01
影响因子：
16.6
通讯作者：
Patel, Dinshaw J.
中科院分区：
文献类型：
--
作者：
Huang, Hongda;Deng, Zhong;Vladimirova, Olga;Wiedmer, Andreas;Lu, Fang;Lieberman, Paul M.;Patel, Dinshaw J.
组蛋白H3.3伴侣DAXX与异染色质的形成和转录沉默有关，特别是对于新感染的DNA病毒基因组进入细胞核。eb病毒（EBV）能在感染细胞的细胞核内以染色质化片段的形式有效地建立稳定的潜伏感染。EBV被膜BNRF1是一种daxx相互作用蛋白，是在潜伏期建立选择性病毒基因表达所必需的。本文报道了BNRF1 DAXX相互作用域（DID）与DAXX组蛋白结合域（HBD）和组蛋白H3.3-H4复合物的结构。BNRF1 DID通过非保守环接触DAXX HBD和组蛋白。BNRF1- daxx接口负责BNRF1定位到pml核体，通常与宿主抗病毒抗性和转录抑制相关。矛盾的是，该界面也是驱动b细胞增殖所需的病毒潜伏周期基因的选择性转录激活所必需的。这些发现揭示了抗病毒组蛋白伴侣的病毒重编程以促进病毒潜伏期和细胞永生的分子细节。Epstein-Barr病毒被膜蛋白BNRF1是在潜伏期建立选择性病毒基因表达所必需的，并与组蛋白伴侣DAXX相互作用。在这里，作者提供了BNRF1如何劫持daxx -组蛋白H3.3-H4复合物的结构见解。
The histone H3.3 chaperone DAXX is implicated in formation of heterochromatin and transcription silencing, especially for newly infecting DNA virus genomes entering the nucleus. Epstein-Barr virus (EBV) can efficiently establish stable latent infection as a chromatinized episome in the nucleus of infected cells. The EBV tegument BNRF1 is a DAXX-interacting protein required for the establishment of selective viral gene expression during latency. Here we report the structure of BNRF1 DAXX-interaction domain (DID) in complex with DAXX histone-binding domain (HBD) and histones H3.3-H4. BNRF1 DID contacts DAXX HBD and histones through non-conserved loops. The BNRF1-DAXX interface is responsible for BNRF1 localization to PML-nuclear bodies typically associated with host-antiviral resistance and transcriptional repression. Paradoxically, the interface is also required for selective transcription activation of viral latent cycle genes required for driving B-cell proliferation. These findings reveal molecular details of virus reprogramming of an antiviral histone chaperone to promote viral latency and cellular immortalization. The Epstein-Barr virus tegument protein BNRF1 is required for the establishment of selective viral gene expression during latency and interacts with the histone chaperone DAXX. Here the authors provide structural insight into how BNRF1 hijacks the DAXX-histone H3.3-H4 complex.
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影响因子：
6.7
作者：
Tsai K;Thikmyanova N;Wojcechowskyj JA;Delecluse HJ;Lieberman PM
通讯作者：
Lieberman PM
影响因子：
10.5
作者：
Drane, Pascal;Ouararhni, Khalid;Hamiche, Ali
通讯作者：
Hamiche, Ali
影响因子：
64.5
作者：
Goldberg AD;Banaszynski LA;Noh KM;Lewis PW;Elsaesser SJ;Stadler S;Dewell S;Law M;Guo X;Li X;Wen D;Chapgier A;DeKelver RC;Miller JC;Lee YL;Boydston EA;Holmes MC;Gregory PD;Greally JM;Rafii S;Yang C;Scambler PJ;Garrick D;Gibbons RJ;Higgs DR;Cristea IM;Urnov FD;Zheng D;Allis CD
通讯作者：
Allis CD
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
DOI：
10.1007/978-1-60761-652-8_30
发表时间：
2010-01-01
期刊：
IN VITRO MUTAGENESIS PROTOCOLS, THIRD EDITION
影响因子：
--
作者：
Tischer, B. Karsten;Smith, Gregory A.;Osterrieder, Nikolaus
通讯作者：
Osterrieder, Nikolaus