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

Sherwin P. Montano, Michael Pierce, Marie L. Coté, Andrew K. Vershon, Millie M. Georgiadis

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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 Å resolution.

Original languageEnglish (US)
Pages (from-to)2127-2130
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number12
DOIs
StatePublished - Dec 1 2002

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ASJC Scopus subject areas

  • Structural Biology

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