Autor: |
Shuey, David J., Parker, Carl S. |
Zdroj: |
Nature; October 1986, Vol. 323 Issue: 6087 p459-461, 3p |
Abstrakt: |
The Drosophila heat-shock transcription factor (HSTF) has been shown to bind to three domains of the heat shock protein 70 gene (hsp 70) control region1,2. The most critical of these for transcrip-tional activation appears to be the one closest to the TATA-homology region2–4. This domain, spanning sequences from −40 to −95, consists of two contiguous HSTF binding sites (sites 1 and 2) that are occupied in a cooperative manner2(see Fig. 1). Recent alkylation interference and protection studies suggest a conformational change occurs in the protein-DNA complex at site 1 upon sequential HSTF binding at site 2 (ref. 5). We report here that HSTF binding to a single site or to both contiguous sites results in the introduction of a specific DNA bend within this domain of the hsp 70 promoter. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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