Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1993-2-26
|
| pubmed:abstractText |
Recent studies have detailed the ability of activating transcription factor-2 (ATF-2) to mediate adenoviral E1a stimulation of gene expression; however, an endogenous regulator for the transcriptional activity of this protein has not been described. To characterize the regulation of ATF-2 activity, we have expressed full-length and truncated peptides corresponding to various regions of the ATF-2 protein in bacteria and the baculovirus insect cell system. Bacterially expressed truncated (350-505) but not full-length ATF-2, was able to bind a consensus cAMP response element-containing oligonucleotide, suggesting the N-terminal moiety may serve as a negative regulator of DNA-binding activity. In contrast, the full-length ATF-2 protein expressed in Spodoptera frugiperda (Sf9) cells using a recombinant baculovirus was fully competent to bind DNA. Protein phosphatase 2A reversed the DNA-binding activity by dephosphorylating the ATF-2 polypeptide. Microtubule-associated protein kinase catalyzed the phosphorylation and stimulated the DNA-binding activity of bacterially expressed full-length ATF-2. Phosphopeptide mapping of phosphorylated ATF-2 proteins identified a single peptide in the N-terminal moiety of ATF-2 phosphorylated by p42 or p54 microtubule-associated protein kinase. Therefore, we propose that phosphorylation of this regulatory site is sufficient to induce an allosteric structural change in the ATF-2 protein, which allows dimerization and subsequent DNA binding.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0888-8809
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
6
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2079-89
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1337144-Amino Acid Sequence,
pubmed-meshheading:1337144-Animals,
pubmed-meshheading:1337144-Baculoviridae,
pubmed-meshheading:1337144-Base Sequence,
pubmed-meshheading:1337144-Binding Sites,
pubmed-meshheading:1337144-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:1337144-Cells, Cultured,
pubmed-meshheading:1337144-DNA,
pubmed-meshheading:1337144-Escherichia coli,
pubmed-meshheading:1337144-Genetic Vectors,
pubmed-meshheading:1337144-Molecular Sequence Data,
pubmed-meshheading:1337144-Moths,
pubmed-meshheading:1337144-Peptide Fragments,
pubmed-meshheading:1337144-Phosphorylation,
pubmed-meshheading:1337144-Protein Kinases,
pubmed-meshheading:1337144-Protein Processing, Post-Translational,
pubmed-meshheading:1337144-Recombinant Fusion Proteins,
pubmed-meshheading:1337144-Transcription Factors,
pubmed-meshheading:1337144-Zinc Fingers
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
Activating transcription factor-2 DNA-binding activity is stimulated by phosphorylation catalyzed by p42 and p54 microtubule-associated protein kinases.
|
| pubmed:affiliation |
Department of Medicine, University of Colorado School of Medicine, Denver 80262.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|