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Papers In Press, published online ahead of print January 18, 2001
Internal Medicine, University of Virginia HSC, Charlottesville, VA 22908
Corresponding Author: wap3g{at}virginia.edu
The hgl5 gene of E. histolytica is negatively regulated through the URE3 DNA motif TATTCTATT. This motif is also present and significant in the function of the E. histolytica fdx gene promoter. A yeast-one-hybrid screen was used to identify an E. histolytica cDNA encoding a protein (URE3-BP) that recognized this DNA motif. Analysis of the predicted amino acid sequence demonstrated the presence of two EF-hand motifs but identified no canonical DNA binding motifs. URE3-BP, expressed in bacteria, demonstrated Ca2+-dependent and sequence-specific recognition of the URE3 DNA sequence as assessed by electrophoretic mobility shift assays. Antibodies raised against URE3-BP blocked the formation of the URE3 DNA protein complex by native nuclear extracts. The URE3-BP protein was present in the E. histolytica nucleus and cytoplasm with an apparent molecular mass of 22.6 kDa. Our results represent the first use of a yeast genetic screen to identify, on the basis of function, a DNA binding protein of an early branching eukaryote. As the URE3 DNA can modulate gene expression in both a positive and negative manner this protein may have more than one mechanism of interaction with transcriptional machinery. Characterization of URE3-BP should provide insight into transcription regulation and virulence control in this parasite.
J. Biol. Chem, 10.1074/jbc.M007375200
Submitted on August 14, 2000
Revised on January 16, 2001
Accepted on January 17, 2001
Identification and characterization of an entamoeba histolytica URE3 sequence-specific DNA binding protein containing EF-hand motifs
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