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A connection between iron–sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica

Department of Bacteriology, University of Wisconsin, 420 Henry Mall, Madison, WI 53706-1502, USA

Correspondence
Diana M. Downs
downs{at}bact.wisc.edu

Several cellular pathways have been identified which affect the efficiency of thiamine biosynthesis in Salmonella enterica. Mutants defective in iron–sulfur (Fe–S) cluster metabolism are less efficient at synthesis of the pyrimidine moiety of thiamine. These mutants are compromised for the conversion of aminoimidazole ribotide (AIR) to 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P), not the synthesis of AIR. The gene product ThiC contains potential ligands for an Fe–S cluster that are required for function in vivo. The conversion of AIR to HMP-P is sensitive to oxidative stress, and variants of ThiC have been identified that have increased sensitivity to oxidative growth conditions. The data are consistent with ThiC or an as-yet-unidentified protein involved in HMP-P synthesis containing an Fe–S cluster required for its physiological function.

A table of primers and a sequence alignment are available as supplementary data with the online version of this paper.

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				M. P. Thorgersen and D. M. Downs Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica Microbiology, January 1, 2009; 155(1): 295 - 304. [Abstract] [Full Text] [PDF]