A truncated herpes simplex virus origin binding protein which contains the carboxyl terminal origin binding domain binds to the origin of replication but does not alter its conformation
Identifieur interne : 004662 ( Main/Merge ); précédent : 004661; suivant : 004663A truncated herpes simplex virus origin binding protein which contains the carboxyl terminal origin binding domain binds to the origin of replication but does not alter its conformation
Auteurs : Erik C. Stabell [États-Unis] ; Paul D. Olivo [États-Unis]Source :
- Nucleic Acids Research [ 0305-1048 ] ; 1993.
Abstract
We have studied the DNA binding properties of a polypeptide consisting of the carboxyl terminal 37% ofUL9, the herpes simplex virus type 1 (HSV-1) origin of replication binding protein. Using a Sindbis virus expression system, we expressed and partially purified this truncated form of UL9 (UL9CT) which contains the site-specific DNA binding domain. UL9CT specifically recognized UL9 binding sites on a 200 base pair DNA fragment containing the HSV origin oris and appeared to bind as a dimer to each site. DNAse I footprint analysis showed that UL9CT protectedthe two high affinity binding sites of oris, but unlike full-length UL9, UL9CT did not induce a conformational change in the origin. Addition of anti-UL9CT antibody to the UL9CT origin complex, however, caused a conformational change in the origin to be evident. Our results suggest that a domain, or domains, in the amino terminus are necessary for a UL9-induced origin conformational change to occur and that UL9–-UL9 interactions between binding sites are involved.
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DOI: 10.1093/nar/21.22.5203
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