scholarly journals Interaction of a DNA-binding protein, the gene product of D5 of bacteriophage T5, with double-stranded DNA. Analysis by metrizamide gradient centrifugation.

1982 ◽  
Vol 257 (24) ◽  
pp. 14811-14816
Author(s):  
R K Fujimura ◽  
B C Roop
1979 ◽  
Vol 29 (1) ◽  
pp. 322-327 ◽  
Author(s):  
D J McCorquodale ◽  
J Gossling ◽  
R Benzinger ◽  
R Chesney ◽  
L Lawhorne ◽  
...  

1988 ◽  
Vol 170 (12) ◽  
pp. 5916-5918 ◽  
Author(s):  
R Aasland ◽  
J Coleman ◽  
A L Holck ◽  
C L Smith ◽  
C R Raetz ◽  
...  

2005 ◽  
Vol 5 (8) ◽  
pp. 1216-1219 ◽  
Author(s):  
Yunfei Bai ◽  
Qinyu Ge ◽  
Quanjun Liu ◽  
Tongxiang Li ◽  
Jinke Wang ◽  
...  

1992 ◽  
Vol 225 (4) ◽  
pp. 999-1011 ◽  
Author(s):  
Maarten H. Stuiver ◽  
Wilma G. Bergsma ◽  
Annika C. Arnberg ◽  
Herbert van Amerongen ◽  
Rienk van Grondelle ◽  
...  

2001 ◽  
Vol 57 (12) ◽  
pp. 1893-1894 ◽  
Author(s):  
Ben N. Wardleworth ◽  
Rupert J. M. Russell ◽  
Malcolm F. White ◽  
Garry L. Taylor

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.


Sign in / Sign up

Export Citation Format

Share Document