Mediator was first identified because of its activity in activator-stimulated transcription in vivo and in vitro. Later, biochemical fractionation led to the co-purification of the multi-subunit Mediator complex and RNA polymerase II (pol II). Results of these studies suggested a model whereby transcription-activator proteins, which bind to specific gene regulatory sequences, recruit both Mediator and pol II as a holoenzyme in a one-step mechanism. More recent studies of Drosophila Mediator and additional studies in yeast have demonstrated that different transcription activators can bind and recruit Mediator to promoters in vivo in a step that is independent of pol II recruitment. Moreover, the different activators in Drosophila bind and recruit Mediator via physical interactions with specific subsets of proteins. These features of Mediator function seem to be broadly conserved.
|Number of pages||5|
|Journal||Trends in Biochemical Sciences|
|Publication status||Published - 2005 May|
Bibliographical noteFunding Information:
We thank Steve Mauro for comments and the NIH (GM25232) and the Creative Research Initiative Program of Korean Ministry of Science and Technology for support.
All Science Journal Classification (ASJC) codes
- Molecular Biology