Source:http://linkedlifedata.com/resource/pubmed/id/12021283
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
30
|
pubmed:dateCreated |
2002-7-22
|
pubmed:abstractText |
The Mediator complex is generally required for transcriptional regulation in species ranging from yeast to human. Throughout evolution, the functional diversity of the Mediator complex has been enhanced to meet the increasing requirements for sophisticated gene regulation. It is likely that greater structural complexity is thus required to accomplish these new, complex regulatory functions. In this study, we took systematic steps to examine various types of Mediator complexes in Drosophila melanogaster. Such efforts led to the identification of three distinct forms of Mediator complexes. In exploring their compositional and functional heterogeneity, we found that the smallest complex (C1) is highly enriched in a certain type of Drosophila cells and possesses novel Mediator proteins. The subunits shared among the three Mediator complexes (C1, C2, and C3) appear to form a stable modular structure that serves as a binding surface for transcriptional activator proteins. However, only C2 and C3 were able to support activated transcription in vitro. These findings suggest that different cell types may require distinct Mediator complexes, some of which may participate in nuclear processes other than the previously identified functions.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
277
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
27154-61
|
pubmed:dateRevised |
2004-11-17
|
pubmed:meshHeading |
pubmed-meshheading:12021283-Amino Acid Sequence,
pubmed-meshheading:12021283-Animals,
pubmed-meshheading:12021283-Blotting, Western,
pubmed-meshheading:12021283-Cell Line,
pubmed-meshheading:12021283-Cell Nucleus,
pubmed-meshheading:12021283-Chromatography, Gel,
pubmed-meshheading:12021283-Culture Media, Serum-Free,
pubmed-meshheading:12021283-Drosophila melanogaster,
pubmed-meshheading:12021283-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12021283-Luciferases,
pubmed-meshheading:12021283-Molecular Sequence Data,
pubmed-meshheading:12021283-Protein Binding,
pubmed-meshheading:12021283-RNA,
pubmed-meshheading:12021283-RNA, Double-Stranded,
pubmed-meshheading:12021283-Transcription, Genetic,
pubmed-meshheading:12021283-Transcription Factors
|
pubmed:year |
2002
|
pubmed:articleTitle |
Novel Mediator proteins of the small Mediator complex in Drosophila SL2 cells.
|
pubmed:affiliation |
National Creative Research Initiative Center for Genome Regulation, Department of Biochemistry, Yonsei University, Seoul 120-749, Korea.
|
pubmed:publicationType |
Journal Article
|