Linked Life Data

10747977

Source:http://linkedlifedata.com/resource/pubmed/id/10747977

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2000-6-21
pubmed:abstractText
A 58-amino acid region mediates the core transactivation activity of the glucocorticoid receptor tau1 activation domain. This tau1 core domain is unstructured in aqueous buffers, but in the presence of trifluoroethanol three alpha-helical segments are induced. Two of these putative structural modules have been tested in different combinations with regard to transactivation potential in vivo and binding capacity to the coactivators in vitro. The results show that whereas single modules are not transcriptionally active, any combination of two or three modules is sufficient, with trimodular constructs having the highest activity. However, proteins containing one, two, or three segments bind Ada2 and cAMP-response element-binding protein with similar affinity. A single segment is thus able to bind a target factor but cannot transactivate target genes significantly. The results are consistent with models in which activation domains are comprised of short activation modules that allow multiple interactions with coactivators. Our results also suggest that an increased number of modules may not result in correspondingly higher affinity but instead that the concentration of binding sites is increased, which gives rise to a higher association rate. This is consistent with a model where the association rate for activator-target factor interactions rather than the equilibrium constant is the most relevant measure of activator potency.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15014-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10747977-Amino Acid Sequence, pubmed-meshheading:10747977-Binding Sites, pubmed-meshheading:10747977-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:10747977-Fungal Proteins, pubmed-meshheading:10747977-Glutathione Transferase, pubmed-meshheading:10747977-Humans, pubmed-meshheading:10747977-Molecular Sequence Data, pubmed-meshheading:10747977-Peptide Fragments, pubmed-meshheading:10747977-Plasmids, pubmed-meshheading:10747977-Protein Structure, Secondary, pubmed-meshheading:10747977-Receptors, Glucocorticoid, pubmed-meshheading:10747977-Recombinant Fusion Proteins, pubmed-meshheading:10747977-Saccharomyces cerevisiae, pubmed-meshheading:10747977-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10747977-Transcription Factors, pubmed-meshheading:10747977-Transcriptional Activation, pubmed-meshheading:10747977-beta-Galactosidase
pubmed:year
2000
pubmed:articleTitle
Architectural principles for the structure and function of the glucocorticoid receptor tau 1 core activation domain.
pubmed:affiliation
Department of Biosciences, Karolinska Institutet, Novum, Huddinge S-141 57, Sweden. anette.warnmark@cbt.ki.se
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't