Linked Life Data

7961904

Source:http://linkedlifedata.com/resource/pubmed/id/7961904

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
1994-12-19
pubmed:abstractText
The herpes simplex virus type 1 (HSV-1) origin binding protein (UL9 protein) interacts specifically with the HSV-1 encoded single strand DNA-binding protein ICP8 (Boehmer, P.E. and Lehman, I.R. (1994) Proc. Natl. Acad. Sci. U.S.A. 90, 8444-8448). A UL9 mutant protein (UL9DM27) that lacks the C-terminal 27 amino acids shows normal origin-specific DNA binding and retains its DNA-dependent ATPase and helicase activities, but has a greatly reduced affinity for ICP8. The extreme C-terminal portion of the UL9 protein is therefore required for ICP8 binding. The helicase activity of the UL9DM27 protein is approximately 8-fold greater than that of the wild type UL9 protein and is not stimulated by ICP8. The UL9DM27 protein has a reduced ability to replicate origin-containing plasmids in vivo. Consequently, the interaction between the UL9 protein and ICP8 is likely to be important for origin-dependent DNA replication in vivo, presumably to promote efficient unwinding of the DNA at an HSV-1 origin of DNA replication.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29329-34
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Association of origin binding protein and single strand DNA-binding protein, ICP8, during herpes simplex virus type 1 DNA replication in vivo.
pubmed:affiliation
Department of Biochemistry, Beckman Center, Stanford University School of Medicine, California 94305.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't