Structural basis underlying viral hijacking of a histone chaperone complex Journal Article
| Authors: | Huang, H.; Deng, Z.; Vladimirova, O.; Wiedmer, A.; Lu, F.; Lieberman, P. M.; Patel, D. J. |
| Article Title: | Structural basis underlying viral hijacking of a histone chaperone complex |
| 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. |
| Keywords: | dna viruses; human herpesvirus 4 |
| Journal Title: | Nature Communications |
| Volume: | 7 |
| ISSN: | 2041-1723 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2016-09-01 |
| Start Page: | 12707 |
| Language: | English |
| DOI: | 10.1038/ncomms12707 |
| PROVIDER: | scopus |
| PMCID: | PMC5025803 |
| PUBMED: | 27581705 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 3 October 2016 -- Source: Scopus |
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