The yeast regulatory protein ADR1 binds in a zinc-dependent manner to the upstream activating sequence of ADH2.
AUTOR(ES)
Eisen, A
RESUMO
The yeast ADR1 protein contains two zinc finger domains that are essential for its role in transcriptional activation of alcohol dehydrogenase (ADH2). These domains are thought to function as DNA-binding structures. An ADR1-beta-galactosidase fusion protein made in Escherichia coli and containing the finger domains of ADR1 binds in vitro in a zinc-dependent manner to DNA fragments containing the two ADH2 upstream activation sequences. The strongest binding is to upstream activation sequence 1, a 22-base-pair palindrome.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=365534Documentos Relacionados
- Two monomers of yeast transcription factor ADR1 bind a palindromic sequence symmetrically to activate ADH2 expression.
- The LIM domains of hic-5 protein recognize specific DNA fragments in a zinc-dependent manner in vitro.
- A novel class of plant-specific zinc-dependent DNA-binding protein that binds to A/T-rich DNA sequences
- Characterization of a zinc-dependent transcriptional activator from Arabidopsis.
- Zinc-dependent dimers observed in crystals of human endostatin