Abstract
Herpes simplex virus type 1 (HSV-1) UL3 protein is a nuclear protein. In this study, the molecular mechanism of the subcellular localization of UL3 was characterized by fluorescence microscopy in living cells. A nuclear localization signal (NLS) and a nuclear export signal (NES) were also identified. UL3 was demonstrated to target to the cytoplasm through the NES via chromosomal region maintenance 1 (CRM-1) dependent pathway, and to the nucleus through RanGTP-dependent mechanism. Heterokaryon assays confirmed that UL3 was capable of shuttling between the nucleus and the cytoplasm. These results demonstrate that the UL3 protein is a novel HSV-1 encoded nucleocytoplasmic shuttling protein.
Copyright © 2011 Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Active Transport, Cell Nucleus
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Amino Acid Sequence
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Animals
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Blotting, Western
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COS Cells
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Cell Nucleus / drug effects
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Cell Nucleus / genetics
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Cell Nucleus / metabolism
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Chlorocebus aethiops
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Cloning, Molecular
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Cytoplasm / drug effects
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Cytoplasm / genetics
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Cytoplasm / metabolism
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Exportin 1 Protein
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Fatty Acids, Unsaturated / pharmacology
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Herpesvirus 1, Human / genetics
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Herpesvirus 1, Human / metabolism*
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Humans
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Karyopherins / metabolism
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Mice
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Microscopy, Fluorescence
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Molecular Sequence Data
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NIH 3T3 Cells
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Nuclear Export Signals*
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Nuclear Localization Signals / metabolism*
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Plasmids / genetics
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Plasmids / metabolism
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Receptors, Cytoplasmic and Nuclear / metabolism
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Deletion
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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Fatty Acids, Unsaturated
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Karyopherins
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Nuclear Export Signals
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Nuclear Localization Signals
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Receptors, Cytoplasmic and Nuclear
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Recombinant Fusion Proteins
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UL3 protein, Human herpesvirus 1
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Viral Proteins
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leptomycin B