Human cytomegalovirus IE1 protein alters the higher-order chromatin structure by targeting the acidic patch of the nucleosome
Abstract
Human cytomegalovirus (hCMV) immediate early 1 (IE1) protein associates with condensed chromatin of the host cell during mitosis. We have determined the structure of the chromatin-tethering domain (CTD) of IE1 bound to the nucleosome core particle, and discovered that IE1-CTD specifically interacts with the H2A-H2B acidic patch and impairs the compaction of higher-order chromatin structure. Our results suggest that IE1 loosens up the folding of host chromatin during hCMV infections.
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Reviewing Editor
- Patrick Cramer, Max Planck Institute for Biophysical Chemistry, Germany
Version history
- Received: September 26, 2015
- Accepted: January 21, 2016
- Accepted Manuscript published: January 26, 2016 (version 1)
- Version of Record published: February 11, 2016 (version 2)
- Version of Record updated: March 14, 2016 (version 3)
Copyright
© 2016, Fang et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Further reading
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- Biochemistry and Chemical Biology
- Microbiology and Infectious Disease
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