Source:http://linkedlifedata.com/resource/pubmed/id/10636877
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2000-2-24
|
| pubmed:abstractText |
The high mobility group I-C (HMGI-C) protein is an abundant component of rapidly proliferating undifferentiated cells. High level expression of this protein is characteristic for early embryonic tissue and diverse tumors. HMGI-C can function as an architectural factor enhancing the activity of transcription factor NF-kappaB on the beta-interferon promoter. The protein has three minor groove DNA-binding domains (AT-hooks). Here, we describe the complex of HMGI-C with a fragment of the beta-interferon promoter. We show that the protein binds to NRDI and PRDII elements of the promoter with its first and second AT-hook, respectively. Phosphorylation by Cdc2 kinase leads to a partial derailing of the AT-hooks from the minor groove, affecting mainly the second binding domain. In contrast, binding to long AT stretches of DNA involves contacts with all three AT-hooks and is marginally sensitive to phosphorylation. Our data stress the importance of conformation of the DNA binding site and protein phosphorylation for its function.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/HMGA2 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-beta
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
21
|
| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1793-801
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| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:10636877-Amino Acid Sequence,
pubmed-meshheading:10636877-Animals,
pubmed-meshheading:10636877-Base Sequence,
pubmed-meshheading:10636877-CDC2 Protein Kinase,
pubmed-meshheading:10636877-DNA,
pubmed-meshheading:10636877-DNA Footprinting,
pubmed-meshheading:10636877-Dose-Response Relationship, Drug,
pubmed-meshheading:10636877-HMGA2 Protein,
pubmed-meshheading:10636877-High Mobility Group Proteins,
pubmed-meshheading:10636877-Interferon-beta,
pubmed-meshheading:10636877-Methylation,
pubmed-meshheading:10636877-Mice,
pubmed-meshheading:10636877-Models, Genetic,
pubmed-meshheading:10636877-Molecular Sequence Data,
pubmed-meshheading:10636877-Phosphorylation,
pubmed-meshheading:10636877-Promoter Regions, Genetic,
pubmed-meshheading:10636877-Protein Binding,
pubmed-meshheading:10636877-Protein Conformation
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| pubmed:year |
2000
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| pubmed:articleTitle |
Architecture of high mobility group protein I-C.DNA complex and its perturbation upon phosphorylation by Cdc2 kinase.
|
| pubmed:affiliation |
III Zoologisches Institut, Entwicklungsbiologie, Universität Göttingen, Humboldtallee 34A, D-37073 Göttingen, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|