A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica.
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.
Dougherty
Michael J
MJ
Department of Bacteriology, University of Wisconsin, 420 Henry Mall, Madison, WI 53706-1502, USA.
Downs
Diana M
DM
Department of Bacteriology, University of Wisconsin, 420 Henry Mall, Madison, WI 53706-1502, USA.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D010269:Paraquat / Q000494:pharmacology; D011743:Pyrimidines / Q000096:biosynthesis*; D012265:Ribonucleotides / Q000378:metabolism; D019779:Salmonella enterica / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism; D013831:Thiamine / Q000378:metabolism
C101901:4-amino-5-hydroxymethyl-2-methylpyrimidine; D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D011743:Pyrimidines; D012265:Ribonucleotides; C105797:ThiC protein, Bacteria; D013481:Superoxides; C024828:aminoimidazole ribotide; D010269:Paraquat; D013831:Thiamine