Linked Life Data

7964616

Source:http://linkedlifedata.com/resource/pubmed/id/7964616

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1994-12-1
pubmed:abstractText
The Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA-2) protein is essential for the immortalization of human primary B cells by EBV. EBNA-2 trans-activates cellular and viral genes like CD23, c-fgr, latent membrane protein 1 (LMP1) and terminal protein 1 (TP1). Trans-activation of the TP1 promoter and of the BamHI C promoter has already been investigated in detail and appears to be mediated via protein-protein interactions and not by direct binding of EBNA-2 type A (of EBV type 1) to the DNA. EBNA-2 is able to trans-activate the expression of the LMP gene in several cell lines. Various reports have delineated the cis-acting elements of the LMP promoter through which EBNA-2 mediates trans-activation. To determine whether EBNA-2 also trans-activates the LMP promoter by protein-protein interactions, we performed a series of gel retardation assays and competition experiments with LMP promoter fragments of different sizes. We determined that the protein-binding region on the LMP promoter was within a 42 bp fragment encompassing nucleotides -135 to -176 relative to the LMP transcriptional start site. None of the DNA fragments investigated indicated interaction of EBNA-2 with the DNA via protein-protein interactions. No significant differences between EBNA-2-positive and EBNA-2-negative nuclear extracts could be seen in the gel retardation assay under conditions that clearly showed binding of EBNA-2A to the TP1 promoter. However, analysis of sucrose gradient fractions in the gel retardation assay provided evidence that the LMP promoter-binding proteins form a complex of higher M(r) in EBNA-2-positive cell extracts. These complexes were destroyed by detergent. We deduce from these results that EBNA-2-positive cells might indeed contain specific complexes bound to the LMP promoter which are, however, too labile to be detected in a standard gel retardation assay.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
75 ( Pt 11)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3067-79
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7964616-Antigens, Viral, pubmed-meshheading:7964616-B-Lymphocytes, pubmed-meshheading:7964616-Base Sequence, pubmed-meshheading:7964616-Cell Line, pubmed-meshheading:7964616-Cell Nucleus, pubmed-meshheading:7964616-DNA Primers, pubmed-meshheading:7964616-DNA-Binding Proteins, pubmed-meshheading:7964616-Epstein-Barr Virus Nuclear Antigens, pubmed-meshheading:7964616-Gene Expression Regulation, Viral, pubmed-meshheading:7964616-Genes, Viral, pubmed-meshheading:7964616-Genome, Viral, pubmed-meshheading:7964616-Herpesvirus 4, Human, pubmed-meshheading:7964616-Humans, pubmed-meshheading:7964616-Molecular Sequence Data, pubmed-meshheading:7964616-Oligodeoxyribonucleotides, pubmed-meshheading:7964616-Polymerase Chain Reaction, pubmed-meshheading:7964616-Protein Biosynthesis, pubmed-meshheading:7964616-Trans-Activators, pubmed-meshheading:7964616-Transcription, Genetic, pubmed-meshheading:7964616-Transcriptional Activation
pubmed:year
1994
pubmed:articleTitle
DNA-binding studies of the Epstein-Barr virus nuclear antigen 2 (EBNA-2): evidence for complex formation by latent membrane protein gene promoter-binding proteins in EBNA-2-positive cell lines.
pubmed:affiliation
Institut für medizinische Mikrobiologie und Hygiene, Universitätskliniken des Saarlandes, Homburg/Saar, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't