Structural basis underlying viral hijacking of a histone chaperone complex

Hongda Huang, Zhong Deng, Olga Vladimirova, Andreas Wiedmer, Fang Lu, Paul M. Lieberman () and Dinshaw J. Patel ()
Additional contact information
Hongda Huang: Structural Biology Program, Memorial Sloan-Kettering Cancer Center
Zhong Deng: Gene Expression and Regulation Program, The Wistar Institute
Olga Vladimirova: Gene Expression and Regulation Program, The Wistar Institute
Andreas Wiedmer: Gene Expression and Regulation Program, The Wistar Institute
Fang Lu: Gene Expression and Regulation Program, The Wistar Institute
Paul M. Lieberman: Gene Expression and Regulation Program, The Wistar Institute
Dinshaw J. Patel: Structural Biology Program, Memorial Sloan-Kettering Cancer Center

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: Abstract 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.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms12707 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12707

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms12707

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().