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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| Publicat a: | Mol Cell Biol |
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| Autors principals: | , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Taylor & Francis
1990
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| Matèries: | |
| Accés en línia: | 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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