Crystal structure of the DNA-binding domain from Ndt80, a transcriptional activator required for meisis in yeast

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

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

Ndt80 is a transcriptional activator required for meiosis in the yeast Saccharomyces cerevisiae. Here, we report the crystal structure at 2.3 Å resolution of the DNA-binding domain of Ndt80 experimentally phased by using the anomalous and isomorphous signal from a single ordered Se atom per molecule of 272-aa residues. The structure reveals a single ≈32-kDa domain with a distinct fold comprising a β-sandwich core elaborated with seven additional β-sheets and three short α-helices. Inspired by the structure, we have performed a mutational analysis and defined a DNA-binding motif in this domain. The DNA-binding domain of Ndt80 is homologous to a number of proteins from higher eukaryotes, and the residues that we have shown are required for DNA binding by Ndt80 are highly conserved among this group of proteins. These results suggest that Ndt80 is the defining member of a previously uncharacterized family of transcription factors, including the human protein (C11orf9), which has been shown to be highly expressed in invasive or metastatic tumor cells.

Original languageEnglish (US)
Pages (from-to)14041-14046
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number22
DOIs
StatePublished - Oct 29 2002

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Keywords

  • β-sandwich
  • Meiotic
  • Sporulation
  • Transcription factor

ASJC Scopus subject areas

  • Genetics
  • General

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