scholarly journals Unwinding of the box I element of a herpes simplex virus type 1 origin by a complex of the viral origin binding protein, single-strand DNA binding protein, and single-stranded DNA

1997 ◽  
Vol 94 (7) ◽  
pp. 2838-2842 ◽  
Author(s):  
S. S.- K. Lee ◽  
I. R. Lehman
2016 ◽  
Vol 35 (4) ◽  
pp. 704-723 ◽  
Author(s):  
E.D. Moiseeva ◽  
N.P. Bazhulina ◽  
Y.G. Gursky ◽  
S.L. Grokhovsky ◽  
A.N. Surovaya ◽  
...  

2005 ◽  
Vol 79 (14) ◽  
pp. 9356-9358 ◽  
Author(s):  
Nina Bacher Reuven ◽  
Sandra K. Weller

ABSTRACT UL12 is a 5′- to 3′-exonuclease encoded by herpes simplex virus type 1 (HSV-1) which degrades single- and double-stranded DNA. UL12 and the single-strand DNA binding protein ICP8 mediate a strand exchange reaction. We found that ICP8 inhibited UL12 digestion of single-stranded DNA but stimulated digestion of double-stranded DNA threefold. The stimulatory effect of ICP8 was independent of a strand exchange reaction; furthermore, the effect was specific to ICP8, as it could not be reproduced by Escherichia coli single-stranded DNA binding protein. The effect of ICP8 on the rate of UL12 double-stranded DNA digestion is attributable to an increase in processivity in the presence of ICP8.


2000 ◽  
Vol 74 (12) ◽  
pp. 5726-5728 ◽  
Author(s):  
Xiaodun He ◽  
I. R. Lehman

ABSTRACT A herpes simplex virus type 1 (HSV-1) OriS analogue in which the A+T sequence linking the box I and II elements was replaced by two single-stranded oligo(dT)s is unwound by the UL9 protein-ICP8 complex. Unwinding of wild-type OriS by the UL9 protein-ICP8 complex was also observed under conditions which destabilize the A+T sequence. These experiments support a model for the unwinding of OriS in which destabilization of the A+T sequence can generate a single-stranded DNA binding site for ICP8, which then associates with the UL9 protein bound to boxes I and II to promote the bidirectional unwinding of OriS.


1989 ◽  
Vol 70 (9) ◽  
pp. 2357-2364 ◽  
Author(s):  
M. Murphy ◽  
P. Schenk ◽  
H. M. Lankinen ◽  
A. M. Cross ◽  
P. Taylor ◽  
...  

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