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.
Highlights
YjgF is a member of the YjgF/YER057c/UK114 family of proteins present in all three domains of life and defines the Cluster of Orthologous Groups 0251 (9)
The TrpDE complex catalyzes the conversion of chorismate to anthranilate while deaminating glutamine, and subsequently TrpD combines anthranilate and phosphoribosyl pyrophosphate (PRPP) to form phosphoribosyl anthranilate and inorganic phosphate (12, 13)
TrpD Is Necessary for PRA Formation in a yjgF Mutant—Results from a number of in vivo growth analyses suggested a requirement for TrpD, but not TrpE, in the formation of PRA in a yjgF mutant strain
Summary
No-carbon E (NCE) medium of Vogel and Bonner (16, 17) with MgSO4 (1 mM) and glucose as a carbon source (11 mM) was used as a minimal medium.
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