Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast

Elizabeth R. Sprague, Michael J. Redd, Alexander D. Johnson, Cynthia Wolberger

Research output: Contribution to journalArticle

Abstract

The Tup1-Ssn6 corepressor complex regulates the expression of several sets of genes, including genes that specify mating type in the yeast Saccharomyces cerevisiae. Repression of mating-type genes occurs when Tup1-Ssn6 is brought to the DNA by the Matα2 DNA-binding protein and assembled upstream of a- and haploid-specific genes. We have determined the 2.3 Å X-ray crystal structure of the C-terminal domain of Tup1 (accesion No. 1ERJ), a 43 kDa fragment that contains seven copies of the WD40 sequence motif and binds to the Matα2 protein. Moreover, this portion of the protein can partially substitute for full-length Tup1 in bringing about transcriptional repression. The structure reveals a seven-bladed β propeller with an N-terminal subdomain that is anchored to the side of the propeller and extends the β sheet of one of the blades. Point mutations in Tup1 that specifically affect the Tup1-Matα2 interaction cluster on one surface of the propeller. We identified regions of Tup1 that are conserved among the fungal Tup1 homologs and may be important in protein-protein interactions with additional components of the Tup1-mediated repression pathways.

Original languageEnglish (US)
Pages (from-to)3016-3027
Number of pages12
JournalEMBO Journal
Volume19
Issue number12
StatePublished - Jun 15 2000

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Keywords

  • Repression
  • Transcriptional regulation
  • Tup1
  • WD40 repeat
  • X-ray crystal structure

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Sprague, E. R., Redd, M. J., Johnson, A. D., & Wolberger, C. (2000). Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast. EMBO Journal, 19(12), 3016-3027.