Human cytomegalovirus IE1 protein alters the higher-order chromatin structure by targeting the acidic patch of the nucleosome
Qianglin Fang,1,2,† Ping Chen,1,† Mingzhu Wang,1 Junnan Fang,1,2 Na Yang,1,2 Guohong Li,1,2,* and Rui-Ming Xu1,2,*

1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
2 College of Life Sciences, University of Chinese Academy of Sciences, Beijing, China.

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 the specific interaction between IE1-CTD and the H2A-H2B acidic patch impairs the compaction of higher-order chromatin structure. Our results suggest that IE1 loosens up the folding of host chromatin during hCMV infections.

See more about this article: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764553/