Linked Life Data

12093179

Source:http://linkedlifedata.com/resource/pubmed/id/12093179

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-7-2
pubmed:abstractText
A previous study shows that Hsp60 not only interacts with, but also activates human hepatitis B virus polymerase, HBV Pol (S. G. Park and G. Jung, 2001, J. Virol. 75, 6962-6968). To provide a more detailed analysis of the relationship between the two proteins, (i) the binding sites on human HBV Pol for Hsp60 and (ii) the effect of pregenomic RNA on human HBV Pol-Hsp60 binding were analyzed. The binding sites on human HBV Pol were mapped with several deletion mutant proteins of the Pol expressed in insect cells by using recombinant baculovirus. Immunoprecipitation of each deletion mutant protein by M2 beads showed that binding of Hsp60 to human HBV Pol requires two minimal sites on human HBV Pol: amino acids 1 to 199 (TP) and amino acids 680 to 842 (RH). Human HBV Pol was also shown to bind to Hsp60 in HepG2 cells, the host cell line for human HBV. In addition, Hsp60 binding to the Pol was found to be dispensable to pregenomic RNA binding to human HBV Pol. Overall, this article infers that Hsp60 activates human HBV Pol through binding at the TP and RH domains of the Pol and the Pol binding to Hsp60 does not require pregenomic RNA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0042-6822
pubmed:author
pubmed:copyrightInfo
(c) 2002 Elsevier Science (USA).
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
298
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
116-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Binding site analysis of human HBV pol for molecular chaperonin, hsp60.
pubmed:affiliation
School of Biological Sciences, Seoul National University, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't