@article {2418,
	title = {Structure and function of CRSP/Med2; a promoter-selective transcriptional coactivator complex.},
	journal = {Molecular Cell},
	volume = {14},
	year = {2004},
	month = {2004 Jun 4},
	pages = {675-83},
	abstract = {<p>The multi-subunit, human CRSP coactivator-also known as Mediator (Med)-regulates transcription by mediating signals between enhancer-bound factors (activators) and the core transcriptional machinery. Interestingly, different activators are known to bind distinct subunits within the CRSP/Med complex. We have isolated a stable, endogenous CRSP/Med complex (CRSP/Med2) that specifically lacks both the Med220 and the Med70 subunits. The three-dimensional structure of CRSP/Med2 was determined to 31 A resolution using electron microscopy and single-particle reconstruction techniques. Despite lacking both Med220 and Med70, CRSP/Med2 displays potent, activator-dependent transcriptional coactivator function in response to VP16, Sp1, and Sp1/SREBP-1a in vitro using chromatin templates. However, CRSP/Med2 is unable to potentiate activated transcription from a vitamin D receptor-responsive promoter, which requires interaction with Med220 for coactivator recruitment, whereas VDR-directed activation by CRSP/Med occurs normally. Thus, it appears that CRSP/Med may be regulated by a combinatorial assembly mechanism that allows promoter-selective function upon exchange of specific coactivator targets.</p>
},
	keywords = {CCAAT-Enhancer-Binding Proteins, DNA-Binding Proteins, Genes, Genetic, Hela Cells, Herpes Simplex Virus Protein Vmw65, Humans, Macromolecular Substances, Promoter Regions, Protein Structure, Protein Subunits, Regulator, Sp1 Transcription Factor, Sterol Regulatory Element Binding Protein 1, Tertiary, Trans-Activators, Transcription Factors, Transcriptional Activation, Vitamin D Response Element},
	issn = {1097-2765},
	doi = {10.1073/pnas.1100640108},
	author = {Taatjes, Dylan J and Tjian, Robert}
}
