The Gcn4p Activation Domain Interacts Specifically In Vitro with RNA Polymerase II Holoenzyme, TFIID, and the Adap-Gcn5p Coactivator Complex

The Gcn4p activation domain contains seven clusters of hydrophobic residues that make additive contributions to transcriptional activation in vivo. We observed efficient binding of a glutathione S-transferase (GST)–Gcn4p fusion protein to components of three different coactivator complexes in Saccha...

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Auteurs principaux: Drysdale, Connie M., Jackson, Belinda M., McVeigh, Richard, Klebanow, Edward R., Bai, Yu, Kokubo, Tetsuro, Swanson, Mark, Nakatani, Yoshihiro, Weil, P. Anthony, Hinnebusch, Alan G.
Format: Artigo
Langue:Inglês
Publié: American Society for Microbiology 1998
Sujets:
Transcriptional Regulation
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC108886/
https://ncbi.nlm.nih.gov/pubmed/9488488
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