Mutations that define the optimal half-site for binding yeast GCN4 activator protein and identify an ATF/CREB-like repressor that recognizes similar DNA sites.

The yeast GCN4 transcriptional activator protein binds as a dimer to a dyad-symmetric sequence, indicative of a protein-DNA complex in which two protein monomers interact with adjacent half-sites. However, the optimal GCN4 recognition site, ATGA(C/G)TCAT, is inherently asymmetric because it contains...

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Vydáno v:	Mol Cell Biol
Hlavní autoři:	Sellers, J W, Vincent, A C, Struhl, K
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Taylor & Francis 1990
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC361174/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2204805/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.10.10.5077-5086.1990
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