期刊
VIRUS RESEARCH
卷 153, 期 1, 页码 71-81出版社
ELSEVIER
DOI: 10.1016/j.virusres.2010.07.009
关键词
Herpes simplex virus 1 US11 protein; Nucleolar localization signal; Nuclear export signal; Ran-GTP; Importin
类别
资金
- Major State Basic Research Development Program of China [2010CB530105]
- Chinese Academy of Sciences [20071010-141]
- National Natural Science Foundation of China [30870120]
- Hubei Province Natural Science Foundation of Innovation [2008CDA013]
The herpes simplex virus type I (HSV-1) US11 protein is an RNA-binding multifunctional regulator that specifically and stably associates with nucleoli. Although the C-terminal part of US11 was responsible for its nucleolar localization, the precise nucleolar localization signal (NoLS) and nuclear export signal (NES) of US11 and its nuclear import and export mechanisms are still elusive. In this study, fluorescence microscopy was employed to investigate the subcellular localization of US11 and characterize its transport mechanism in living cells. By constructing a series of deletion mutants fused with enhanced yellow fluorescent protein (EYFP), three novel NoLSs of US11 were for the first time mapped to amino acids 84-125, 126-152, and 89-146, respectively. Additionally, the NES was identified to locate between amino acids 89 and 119. Furthermore, the US11 protein was demonstrated to target to the cytoplasm through the NES by chromosomal region maintenance 1 (CRM1)-independent pathway, and to the nucleolus through Ran and importin beta-dependent mechanism that does not require importin alpha 5. (C) 2010 Elsevier B.V. All rights reserved.
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