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Crystallographic studies of a novel DNA-binding domain from the yeast transcriptional activator Ndt80.

Authors :
Montano SP
Pierce M
Coté ML
Vershon AK
Georgiadis MM
Source :
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2002 Dec; Vol. 58 (Pt 12), pp. 2127-30. Date of Electronic Publication: 2002 Nov 23.
Publication Year :
2002

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.

Details

Language :
English
ISSN :
0907-4449
Volume :
58
Issue :
Pt 12
Database :
MEDLINE
Journal :
Acta crystallographica. Section D, Biological crystallography
Publication Type :
Academic Journal
Accession number :
12454476
Full Text :
https://doi.org/10.1107/s0907444902015020