Linked Life Data

1657954

Source:http://linkedlifedata.com/resource/pubmed/id/1657954

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1991-12-13
pubmed:abstractText
Herpes simplex virus type 1 (HSV-1) encodes a heterotrimeric helicase-primase comprised of the products of the UL5, UL8, and UL52 genes (Crute, J. J., and Lehman, I. R. (1991) J. Biol. Chem. 266, 4484-4488). A steady state kinetic analysis of the enzyme isolated from HSV-1-infected CV-1 cells or insect cells expressing the enzyme after infection with recombinant baculoviruses has shown it to possess two sites capable of hydrolyzing nucleoside triphosphates in a DNA-dependent manner. One site (Site I) hydrolyzes both ATP and GTP; the second (Site II) hydrolyzes only ATP. These two sites are contained within a subassembly of the helicase-primase formed by coexpression of the UL5 and UL52 genes in insect cells. Sites I and II are activated by separate DNA effector sites, both of which support DNA helicase action. These findings are likely to be of importance in understanding how helicases in general catalyze the unwinding of duplex DNA and, in particular, how the helicase-primase functions at the HSV-1 replication fork.
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
5
pubmed:volume
266
pubmed:geneSymbol
UL5, UL52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21252-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Herpes simplex-1 helicase-primase. Identification of two nucleoside triphosphatase sites that promote DNA helicase action.
pubmed:affiliation
Department of Biochemistry, Beckman Center, Stanford University School of Medicine, California 94305-5307.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't