scholarly journals The human DnaJ protein, hTid-1, enhances binding of a multimer of the herpes simplex virus type 1 UL9 protein to oris, an origin of viral DNA replication

2002 ◽  
Vol 99 (4) ◽  
pp. 1894-1898 ◽  
Author(s):  
C.-Y. Eom ◽  
I. R. Lehman
2008 ◽  
Vol 89 (7) ◽  
pp. 1709-1715 ◽  
Author(s):  
Martin R. Higgs ◽  
Valerie G. Preston ◽  
Nigel D. Stow

The UL15, UL28 and UL33 proteins of herpes simplex virus type 1 (HSV-1) are thought to comprise a terminase complex responsible for cleavage and packaging of the viral genome into pre-assembled capsids. Immunofluorescence studies confirmed that shortly after infection with wild-type HSV-1 these three proteins localize to viral DNA replication compartments within the nucleus, identified by the presence of the single-stranded DNA-binding protein, ICP8. In cells infected with either UL28- or UL33-null mutants, the other two terminase proteins also co-localized with ICP8. In contrast, neither UL28 nor UL33 was detectable in replication compartments following infection with a UL15-null mutant, although Western blot analysis showed they were present in normal amounts in the infected cells. Provision of UL15 in a complementing cell line restored the ability of all three proteins to localize to replication compartments. These data indicate that UL15 plays a key role in localizing the terminase complex to DNA replication compartments, and that it can interact independently with UL28 and UL33.


Virology ◽  
1980 ◽  
Vol 101 (1) ◽  
pp. 10-24 ◽  
Author(s):  
Louis E. Holland ◽  
Kevin P. Anderson ◽  
Charles Shipman ◽  
Edward K. Wagner

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