scholarly journals The Catalytic Subunit of Herpes Simplex Virus Type 1 DNA Polymerase Contains a Nuclear Localization Signal in the UL42-Binding Region

Virology ◽  
2000 ◽  
Vol 273 (1) ◽  
pp. 139-148 ◽  
Author(s):  
Arianna Loregian ◽  
Elisa Piaia ◽  
Enrico Cancellotti ◽  
Emanuele Papini ◽  
Howard S. Marsden ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Polymerase ◽  
Nuclear Localization ◽  
Herpes Simplex Virus Type ◽  
Nuclear Localization Signal ◽  
Binding Region ◽  
Localization Signal ◽  
Simplex Virus

scholarly journals Differential Intracellular Compartmentalization of Herpetic Thymidine Kinases (TKs) in TK Gene-Transfected Tumor Cells: Molecular Characterization of the Nuclear Localization Signal of Herpes Simplex Virus Type 1 TK

1998 ◽  
Vol 72 (12) ◽  
pp. 9535-9543 ◽  
Author(s):  
Bart Degrève ◽  
Magnus Johansson ◽  
Erik De Clercq ◽  
Anna Karlsson ◽  
Jan Balzarini
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Tumor Cells ◽  
Nuclear Localization ◽  
Herpes Simplex Virus Type ◽  
Nuclear Localization Signal ◽  
Localization Signal ◽  
Simplex Virus ◽  
Hsv 1

ABSTRACT The thymidine kinases (TKs) of herpes simplex virus type 1 (HSV-1), HSV-2, and varicella-zoster virus (VZV) were expressed in human osteosarcoma cells as fusion proteins with the green fluorescent protein (GFP), and their intracellular localizations were determined. The three TK-GFP fusion products were localized in different subcellular compartments of the transfected tumor cells. HSV-1 TK-GFP was localized exclusively in the nucleus, HSV-2 TK-GFP was predominantly found in the cytosol, while VZV TK-GFP was localized in both the nucleus and the cytosol. In support of these findings, we identified a nuclear localization signal (NLS) in the N-terminal arginine-rich region of HSV-1 TK that was absent in HSV-2 and VZV TK. The first 34 amino acids proved necessary for the specific nuclear localization of HSV-1 TK and, when added to the VZV TK-GFP gene construct, also sufficed to specifically target VZV TK-GFP to the nucleus. Further analysis of this NLS through site-directed mutagenesis revealed that the basic amino acid-rich nonapeptide25R-R-T-A-L-R-P-R-R33 is of crucial importance in the nuclear targeting of HSV-1 TK. In particular, we revealed that the presence of the arginine residues at positions 25, 26, 30, 32, and 33 is obligatory for efficient NLS functioning, whereas arginine and histidine residues outside of the nonapeptide (i.e., residues R18, R20, and H22) did not change the functional properties of the NLS.

scholarly journals RNA Binding by the Herpes Simplex Virus Type 1 Nucleocytoplasmic Shuttling Protein UL47 Is Mediated by an N-Terminal Arginine-Rich Domain That Also Functions as Its Nuclear Localization Signal

2006 ◽  
Vol 81 (5) ◽  
pp. 2283-2296 ◽  
Author(s):  
Michelle Donnelly ◽  
Janneke Verhagen ◽  
Gillian Elliott
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Infected Cell ◽  
Nuclear Localization ◽  
Nuclear Localization Signal ◽  
Rna Binding ◽  
Localization Signal ◽  
Simplex Virus

ABSTRACT The function of the alphaherpesvirus UL47 tegument protein has not yet been defined. Nonetheless, previous studies with transfected cells have shown that both the herpes simplex virus type 1 homologue (hUL47, or VP13/14) and the bovine herpesvirus type 1 (BHV-1) homologue (bUL47, or VP8) have the capacity to shuttle between the nucleus and the cytoplasm. Furthermore, hUL47 packaged into the virion has also been shown to bind several individual virus-specific RNA transcripts. Here, we extend these observations and show that hUL47 binds a wide range of RNA species in vitro. It has a high affinity for polyadenylated transcripts but has no apparent selectivity for virus-encoded RNA over cellular RNA. We also show that the virion population of bUL47 binds RNA in vitro. However, while purified recombinant hUL47 retains its RNA binding activity, recombinant bUL47 does not, suggesting that the BHV-1 homologue may require virus-induced modification for its activity. We identify the minimal RNA binding domain in hUL47 as a 26-residue N-terminal peptide containing an arginine-rich motif that is essential but not sufficient for optimal RNA binding, and we demonstrate that this RNA binding domain incorporates the hUL47 minimal nuclear localization signal. In addition, we show that soon after hUL47 is expressed during infection, it colocalizes in the infected cell nucleus with ICP4, the major virus transcriptional activator. Using RNA immunoprecipitations, we demonstrate that hUL47 is also bound in vivo to at least one viral transcript, the ICP0 mRNA. Taken together, these results suggest that hUL47 may play a role in RNA biogenesis in the infected cell.

scholarly journals Role of the Carboxy Terminus of Herpes Simplex Virus Type 1 DNA Polymerase in its Interaction With UL42

1994 ◽  
Vol 75 (11) ◽  
pp. 3127-3135 ◽  
Author(s):  
H. S. Marsden ◽  
M. Murphy ◽  
G. L. McVey ◽  
K. A. MacEachran ◽  
A. M. Owsianka ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Polymerase ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Carboxy Terminus ◽  
Simplex Virus

scholarly journals Effect of spermine on the activity of herpes simplex virus type 1 DNA polymerase

FEBS Letters ◽  
1981 ◽  
Vol 126 (2) ◽  
pp. 157-160 ◽  
Author(s):  
Heather M. Wallace ◽  
Herbert N. Baybutt ◽  
Colin K. Pearson ◽  
Hamish M. Keir
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Polymerase ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Simplex Virus
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