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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A novel docking site on Mediator is critical for activation by VP16 in mammalian cells.

ARC92/ACID1 was identified as a novel specific target of the herpes simplex transactivator VP16 using an affinity purification procedure. Characterization of the protein revealed tight interactions with human Mediator mediated through a von Willebrand type A domain. ARC92/ACID1 further contains a novel activator-interacting domain (ACID), which it shares with at least one other human gene termed PTOV1/ACID2. The structure of ARC92/ACID1 is of ancient origin but is conserved in mammals and in selected higher eukaryotes. A subpopulation of Mediator is associated with ARC92/ACID1, which is specifically required for VP16 activation both in vitro and in mammalian cells, but is dispensable for other activators such as SP1. Despite many known targets of VP16, ARC92/ACID1 appears to impose a critical control on transcription activation by VP16 in mammalian cells.[1]

References

  1. A novel docking site on Mediator is critical for activation by VP16 in mammalian cells. Mittler, G., Stühler, T., Santolin, L., Uhlmann, T., Kremmer, E., Lottspeich, F., Berti, L., Meisterernst, M. EMBO J. (2003) [Pubmed]
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