Linked Life Data

2506451

Source:http://linkedlifedata.com/resource/pubmed/id/2506451

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6239
pubmed:dateCreated
1989-10-13
pubmed:abstractText
The TPA (12-O-tetradecanoyl-phorbol-13-acetate) responsive element (TRE) is recognized by the inducible transcription factor AP1, a heterodimeric complex of Fos- and Jun-protein subunits, which each contain a specific structure known as the leucine zipper through which they interact. Studies using site-directed mutagenesis have shown that a basic region adjacent to the leucine zipper in Fos is crucial for the interaction of the Fos-Jun complex with the TRE, and probably represents a site of interaction with DNA. The functionally crucial amino acids in this region are almost completely conserved between Fos and Jun (refs 6, 7 and 11; M.N. and R.M., unpublished results), indicating the formation of a nearly symmetrical DNA-binding site in the Fos-Jun complex. Whereas Jun can form a homodimeric protein complex which binds to the TRE, Fos is unable to do so. The Fos-Jun heterodimer, however, possesses at least a 30-fold-higher affinity for the TRE than does the Jun-Jun homodimer, indicating cooperative binding. Because Fos cannot form a homodimer it is not known whether Fos specifically recognizes part of the TRE or has a different role in the binding of the Fos-Jun complex to DNA. Here we report that exchanging the leucine zipper in Fos with that of Jun generates a protein (termed psi-Fos) that can form a complex with Fos. This Fos-psi-Fos complex, and to a lesser extent a homodimeric psi-Fos complex, exhibits specific binding to the TRE. This finding strongly supports the hypothesis that Fos and Jun form a nearly symmetrical DNA-binding site that interacts with the palindromic TRE.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
341
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
243-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
A Fos protein containing the Jun leucine zipper forms a homodimer which binds to the AP1 binding site.
pubmed:affiliation
Institut für Molekularbiologie und Tumorforschung, Phillipps-Universität Marburg, FRG.
pubmed:publicationType
Journal Article, In Vitro