Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-8-1
pubmed:abstractText
The EBNA-LP protein encoded by the open reading frame in the leader exons of the Epstein-Barr nuclear antigen messages is essential for efficient immortalization of B lymphocytes. Protein-protein interaction studies using affinity precipitation of proteins from [35S]methionine-labeled cell lysates and bacterially expressed maltose binding protein EBNA-LP fusions were performed. A cellular 68/72-kDa doublet protein was detected. This banding pattern was shown to be identical to that obtained in affinity precipitations with fusions of glutathione-S-transferase and Sp1 (a basal transcription factor). For both EBNA-LP and Sp1 the specific interacting cellular proteins have been identified as heat shock proteins (HSP) 72/73. Affinity precipitation of HSP 72/73 with deletion mutants of EBNA-LP maps the interaction domain on EBNA-LP to exon Y2 which is required for immortalization. Immunoprecipitation of EBNA-LP from EBV-positive lymphoblastoid cell lines coprecipitated the HSP 72/73 proteins, indicating that the interaction occurs in vivo as well as in vitro. The association of HSPs with a widening range of nuclear proteins involved in gene expression and proliferation control now includes Sp1 and EBNA-LP and suggests that there is a central role for molecular chaperones in these processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
91-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Protein-protein interactions between Epstein-Barr virus nuclear antigen-LP and cellular gene products: binding of 70-kilodalton heat shock proteins.
pubmed:affiliation
Department of Infectious Diseases and Microbiology, Graduate School of Public Health, University of Pittsburgh, Pennsylvania 15261, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't