NDLI: The transactivating effect of HSV-1 ICP0 is enhanced by its interaction with the PCAF component of histone acetyltransferase

Content Provider	Springer Nature Link
Author	Li, Weizhong Cun, Wei Liu, Longding Hong, Min Wang, Lei Wang, Lichun Dong, Chenghong Li, Qihan
Copyright Year	2009
Abstract	ICP0 is a multifunctional protein that plays diverse roles in herpes simplex virus type 1 (HSV-1) infection. It can promote the lytic replication of HSV-1 and activate a variety of viral or cellular genes when introduced into cells by transfection or infection. However, the exact mechanism of ICP0 action is not fully understood. In the present study, we observed the co-localization of ICP0 and PCAF (P300/CBP-associated factor), a component of histone acetyltransferase (HAT), in the ND10 (nuclear dot 10) nuclear body. We further confirmed the interaction between ICP0 and PCAF via yeast two-hybrid assay, co-immunoprecipitation, and histone acetyltransferase assays. Analysis of the functional significance of this interaction suggested that PCAF improved the ability of ICP0 to activate transcription of viral genes. Using chromatin immunoprecipitation (ChIP) assays, we observed ICP0-enhanced histone acetylation levels in both viral and cellular gene promoters. Our study suggests that ICP0 regulates transcription through specific interaction with PCAF.
Starting Page	1755
Ending Page	1764
Page Count	10
File Format	PDF
ISSN	03048608
Journal	Archives of Virology
Volume Number	154
Issue Number	11
e-ISSN	14328798
Language	English
Publisher	Springer Vienna
Publisher Date	2009-10-07
Publisher Place	Vienna
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Infectious Diseases Medical Microbiology Virology
Content Type	Text
Resource Type	Article
Subject	Virology Medicine

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