Members of the YjgF/YER057c/UK114 Family of Proteins Inhibit Phosphoribosylamine Synthesis in Vitro |
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Authors: | Jennifer A Lambrecht Beth Ann Browne Diana M Downs |
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Institution: | From the Department of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706 |
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Abstract: | The YjgF/YER057c/UK114 family of proteins is highly conserved across all three domains of life and currently lacks a consensus biochemical function. Analysis of Salmonella enterica strains lacking yjgF has led to a working model in which YjgF functions to remove potentially toxic secondary products of cellular enzymes. Strains lacking yjgF synthesize the thiamine precursor phosphoribosylamine (PRA) by a TrpD-dependent mechanism that is not present in wild-type strains. Here, PRA synthesis was reconstituted in vitro with anthranilate phosphoribosyltransferase (TrpD), threonine dehydratase (IlvA), threonine, and phosphoribosyl pyrophosphate. TrpD-dependent PRA formation in vitro was inhibited by S. enterica YjgF and the human homolog UK114. Thus, the work herein describes the first biochemical assay for diverse members of the highly conserved YjgF/YER057c/UK114 family of proteins and provides a means to dissect the cellular functions of these proteins. |
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Keywords: | Bacterial Genetics Bacterial Metabolism Purine Pyridoxal Phosphate Thiamine TrpD YjgF/YER057c/UK114 Anthranilate Phosphoribosyl Transferase Phosphoribosylamine |
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