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Papers In Press, published online ahead of print December 10, 2003
Département de Biochimie (Biochemistry), Université de Sherbrooke, Faculty of Medicine, Sherbrooke, QC J1H 5N4
Corresponding Author: Simon.Labbe{at}USherbrooke.ca
The Schizosaccharomyces pombe fep1+ gene encodes a GATA transcription factor that represses the expression of iron transport genes in response to elevated iron concentrations. This transcriptional response is altered only in strains harboring a combined deletion of both tup11+ and tup12+ genes. This suggests that Tup11 is capable of negatively regulating iron transport gene expression in the absence of Tup12 and vice versa. The tup11+- and tup12+-encoded proteins resemble the Saccharomyces cerevisiae Tup1 corepressor. Using yeast two-hybrid analysis we show that Tup11 and Fep1 physically interact with each other. The carboxyl-terminal region from amino acids 242 to 564 of Fep1 is required for interaction with Tup11. Within this region, a minimal domain encompassing amino acids 405 to 541 was sufficient for Tup11-Fep1 association. Deletion mapping analysis revealed that the WD40-repeat sequence motifs of Tup11 are necessary for its interaction with Fep1. Analysis of Tup11 mutants with single amino acid substitutions in the WD40 repeats suggested that the Fep1 transcription factor interacts with a putative flat upper surface on the predicted beta-propeller structure of this motif. Further analysis by in vivo coimmunoprecipitation showed that Tup11 and Fep1 are physically associated. In vitro pull-down experiments further verified a direct interaction between the Fep1 carboxyl terminus and the Tup11 carboxyl-terminal WD40 repeat domain. Taken together, these results describe the first example of a physical interaction between a corepressor and an iron-sensing factor controlling the expression of iron uptake genes.
J. Biol. Chem, 10.1074/jbc.M312787200
Submitted on November 24, 2003
Revised on December 10, 2003
Accepted on December 10, 2003
The Schizosaccharomyces pombe corepressor Tup11 interacts with the iron-responsive transcription factor Fep1
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