Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-2-24
pubmed:abstractText
Three related clones encoding proteins (ATFa1, 2 and 3) with specific ATF/CRE DNA-binding activities have been isolated from HeLa cell cDNA libraries. All three isoforms have weak effects on the basal activity of the adenovirus E2a promoter. We present evidence suggesting that a C-terminal element of the ATFa molecules negatively interferes with the intrinsic activation function of these proteins. We also show that coexpression of ATFa with c-Jun, Jun-B or Jun-D stimulates ATFa-dependent reporter activity, while coexpression of c-Fos has no effect. Deletion analyses indicate that the metal-binding region of ATFa is dispensible for this effect, but that the domain comprising the leucine-zipper region of ATFa is required. Reciprocal co-immunoprecipitation experiments and electrophoretic band-shift assays with in vitro synthesized proteins reveal direct interactions between ATFa and Jun or Fos. The ATFa/c-Jun heterodimers, but not the ATFa/c-Fos complexes, bind efficiently to ATF, CRE or AP1 sites. The detection of ATFa-Jun complexes in crude extracts from HeLa cells transfected with ATFa and c-Jun expression vectors suggests that such ATFa/c-Jun heterodimers also form in vivo. Altogether these results indicate that the ATFa proteins may contribute to the modulation of the activity of the Jun/Fos complexes by altering their DNA-binding and transcriptional properties.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
375-85
pubmed:dateRevised
2010-2-4
pubmed:meshHeading
pubmed-meshheading:8290251-Activating Transcription Factors, pubmed-meshheading:8290251-Amino Acid Sequence, pubmed-meshheading:8290251-Animals, pubmed-meshheading:8290251-Base Sequence, pubmed-meshheading:8290251-Blood Proteins, pubmed-meshheading:8290251-Cell Line, pubmed-meshheading:8290251-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:8290251-DNA, pubmed-meshheading:8290251-Genes, Reporter, pubmed-meshheading:8290251-Genes, fos, pubmed-meshheading:8290251-Genes, jun, pubmed-meshheading:8290251-Genetic Vectors, pubmed-meshheading:8290251-HeLa Cells, pubmed-meshheading:8290251-Humans, pubmed-meshheading:8290251-Isomerism, pubmed-meshheading:8290251-Leucine Zippers, pubmed-meshheading:8290251-Molecular Sequence Data, pubmed-meshheading:8290251-Proto-Oncogene Proteins c-fos, pubmed-meshheading:8290251-Proto-Oncogene Proteins c-jun, pubmed-meshheading:8290251-Transcription, Genetic, pubmed-meshheading:8290251-Transcription Factors, pubmed-meshheading:8290251-Transfection
pubmed:year
1994
pubmed:articleTitle
Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family and modulate its transcriptional activity.
pubmed:affiliation
Laboratoire de Génétique Moléculaire des Eucaryotes (CNRS), Unité 184 (INSERM), Institut de Chimie Biologique, Strasbourg, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't