rdf:type |
|
lifeskim:mentions |
umls-concept:C0009015,
umls-concept:C0033684,
umls-concept:C0079686,
umls-concept:C0439851,
umls-concept:C1141625,
umls-concept:C1145667,
umls-concept:C1332119,
umls-concept:C1511573,
umls-concept:C1552596,
umls-concept:C1705772,
umls-concept:C1947931
|
pubmed:issue |
4
|
pubmed:dateCreated |
1990-5-18
|
pubmed:abstractText |
The proto-oncogene products Fos and Jun form a stable heterodimeric complex that functions in transcriptional regulation by interacting with the DNA sequence known as the AP-1 site. Dimer formation occurs through the leucine zipper, a structural motif involving a heptad repeat of leucine residues that is conserved in several fos- and jun-related genes. We have employed a novel cloning strategy to isolate genes encoding proteins capable of forming complexes with Jun. The procedure involves direct screening of a lambda gt11 cDNA library with a biotinylated Jun polypeptide. One clone isolated in this manner encodes CRE-BP1, a leucine zipper-containing protein that binds to the cyclic AMP response element (CRE) as a homodimer. CRE-BP1 also forms heterodimers with Jun but not with Fos. Jun binds cooperatively to the CRE in association with CRE-BP1. Thus, the DNA-binding specificity and affinity of Jun are modulated by association with Fos or with CRE-BP1.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0950-9232
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
5
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
451-8
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:2139203-Animals,
pubmed-meshheading:2139203-Base Sequence,
pubmed-meshheading:2139203-Cell Line,
pubmed-meshheading:2139203-Cloning, Molecular,
pubmed-meshheading:2139203-Cyclic AMP Response Element-Binding Protein,
pubmed-meshheading:2139203-DNA Probes,
pubmed-meshheading:2139203-DNA-Binding Proteins,
pubmed-meshheading:2139203-Gene Library,
pubmed-meshheading:2139203-Macromolecular Substances,
pubmed-meshheading:2139203-Molecular Sequence Data,
pubmed-meshheading:2139203-Oligonucleotide Probes,
pubmed-meshheading:2139203-Polymerase Chain Reaction,
pubmed-meshheading:2139203-Protein Binding,
pubmed-meshheading:2139203-Protein-Tyrosine Kinases,
pubmed-meshheading:2139203-Proto-Oncogene Proteins,
pubmed-meshheading:2139203-Proto-Oncogene Proteins c-fos,
pubmed-meshheading:2139203-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:2139203-Proto-Oncogenes,
pubmed-meshheading:2139203-Rats,
pubmed-meshheading:2139203-Transcription Factors
|
pubmed:year |
1990
|
pubmed:articleTitle |
Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1.
|
pubmed:affiliation |
Department of Molecular Oncology & Virology, Roche Institute of Molecular Biology, Nutley, New Jersey 07110.
|
pubmed:publicationType |
Journal Article
|