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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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Библиографические подробности
Главные авторы: Sellers, J W, Vincent, A C, Struhl, K
Формат: Artigo
Язык:Inglês
Опубликовано: 1990
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC361174/
https://ncbi.nlm.nih.gov/pubmed/2204805
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