Linked Life Data

8409938

Source:http://linkedlifedata.com/resource/pubmed/id/8409938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-11-16
pubmed:abstractText
By immunoprecipitating protein products from virus-infected baby rat kidney (BRK) cells with specific antibodies, we found that the smaller, 243 residue (243R) E1A protein of human adenovirus 5 (Ad5) activated expression of the virus genes for E1B 55K, E2A 72K, E3 19K, hexon, fibre and penton base and the cellular gene for PCNA. The 243R protein also activated the E2A 72K gene in several rodent cell lines. In transient expression assays, this protein trans-activated the E2 early and major late promoters, suggesting that its effect was at least partially transcriptional. Similar assays with mutants of the E2 early promoter suggested that the ATF- and distal E2F-binding sites were required for this activation. Using mutant viruses with deletions in E1A, we found evidence for three separate pathways by which the 243R protein activated gene expression: one depended on sequences in exon 1 required for this protein to bind to p300, a second depended on sequences in exon 1 required for the protein to bind to pRb and the third appeared to be independent of exon 1 altogether and to depend on exon 2. The relative importance of these pathways for activation varied with the gene and cell. We conclude that a major role of E1A in the transformation of BRK cells by Ad5 is to activate specific genes by at least the first two pathways.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
74 ( Pt 10)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2131-41
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Multiple pathways for gene activation in rodent cells by the smaller adenovirus 5 E1A protein and their relevance to growth and transformation.
pubmed:affiliation
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't