A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica
A connection between iron-sulfur cluster metabolism and the biosynthesis of 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate in Salmonella enterica
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DOI：
10.1099/mic.0.28926-0
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发表时间：
2006-08-01
期刊：
影响因子：
2.8
通讯作者：
Downs, Diana M.
中科院分区：
文献类型：
--
作者：
Dougherty, Michael J.;Downs, Diana M.
已经确定了几种影响肠沙门氏菌硫胺素生物合成效率的细胞途径。铁硫（Fe-S）簇代谢缺陷的突变体在合成硫胺素的嘧啶部分时效率较低。这些突变体在将氨基咪唑核糖肽（AIR）转化为4-氨基-5-羟甲基-2-甲基嘧啶磷酸（HMP-P）时受损，而不是AIR的合成。基因产物ti含有Fe-S簇的潜在配体，这是体内功能所必需的。AIR向HMP-P的转化对氧化应激敏感，并且已经确定了对氧化生长条件的敏感性增加的thc变体。这些数据与thc或一种参与HMP-P合成的尚未确定的蛋白质一致，该蛋白质含有其生理功能所需的Fe-S簇。
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.