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Cooperative binding interactions required for function of the Ty1 sterile responsive element
1Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill 27599-7260, USA.
Molecular and Cellular Biology
|August 1, 1997
Summary
Researchers identified two proteins, Ste12p and a 72 kDa protein, that bind to the Ty1 sterile response element (SRE). Tec1p is crucial for forming this complex, revealing new combinatorial transcriptional regulation in Saccharomyces cerevisiae.
Area of Science:
- Molecular Biology
- Yeast Genetics
- Transcriptional Regulation
Background:
- Ste12p transcription factor regulates mating genes and Ty1 element expression in Saccharomyces cerevisiae.
- Ste12p binding sites are pheromone response elements (PREs).
- Some upstream activating sequences (UASs) require multiple PREs or a PRE combined with another protein's binding site.
Purpose of the Study:
- To investigate the protein-DNA interactions at the Ty1 sterile response element (SRE).
- To elucidate the role of Tec1p in the formation of the Ty1 SRE complex.
- To understand combinatorial transcriptional regulation involving Ste12p.
Main Methods:
- UV cross-linking analysis to identify DNA-binding proteins.
- Characterization of protein-DNA complex formation.
- Biochemical assays to determine protein presence in the complex.
Main Results:
- Two proteins, Ste12p and a ~72 kDa protein, directly bind to the Ty1 SRE.
- Tec1p is essential for the formation of the Ty1 SRE protein-DNA complex.
- Tec1p is physically part of the Ty1 SRE complex.
Conclusions:
- Tec1p plays a direct role in the Ty1 SRE.
- This study reveals a novel mechanism of combinatorial transcriptional regulation involving Ste12p and Tec1p.
- The findings contribute to understanding gene expression control in yeast.