1. Crystallographic studies of a novel DNA-binding domain from the yeast transcriptional activator Ndt80.
- Author
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Montano SP, Pierce M, Coté ML, Vershon AK, and Georgiadis MM
- Subjects
- Crystallography, X-Ray, DNA-Binding Proteins metabolism, Electrophoretic Mobility Shift Assay, Hydrolysis, Protein Conformation, Saccharomyces cerevisiae Proteins metabolism, Transcription Factors metabolism, DNA metabolism, DNA-Binding Proteins chemistry, Saccharomyces cerevisiae chemistry, Saccharomyces cerevisiae Proteins chemistry, Transcription Factors chemistry
- Abstract
The Ndt80 protein is a transcriptional activator that plays a key role in the progression of the meiotic divisions in the yeast Saccharomyces cerevisiae. Ndt80 is strongly induced during the middle stages of the sporulation pathway and binds specifically to a promoter element called the MSE to activate transcription of genes required for the meiotic divisions. Here, the preliminary structural and functional studies to characterize the DNA-binding activity of this protein are reported. Through deletion analysis and limited proteolysis studies of Ndt80, a novel 32 kDa DNA-binding domain that is sufficient for DNA-binding in vitro has been defined. Crystals of the DNA-binding domain of Ndt80 in two distinct lattices have been obtained, for which diffraction data extend to 2.3 A resolution.
- Published
- 2002
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