Structural basis underlying viral hijacking of a histone chaperone complex

Hongda Huang; Zhong Deng; Olga Vladimirova; Andreas Wiedmer; Fang Lu; Paul M. Lieberman; Dinshaw J. Patel

doi:10.1038/ncomms12707

Nature Communications (Sep 2016)

Structural basis underlying viral hijacking of a histone chaperone complex

Hongda Huang,
Zhong Deng,
Olga Vladimirova,
Andreas Wiedmer,
Fang Lu,
Paul M. Lieberman,
Dinshaw J. Patel

Affiliations

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

DOI: https://doi.org/10.1038/ncomms12707
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 10

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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