CHARACTERIZATION OF THE FERROUS IRON UPTAKE SYSTEM OF ESCHERICHIA-COLI
CHARACTERIZATION OF THE FERROUS IRON UPTAKE SYSTEM OF ESCHERICHIA-COLI
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DOI：
10.1128/jb.175.19.6212-6219.1993
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发表时间：
1993-10-01
影响因子：
3.2
通讯作者：
HANTKE, K
中科院分区：
文献类型：
--
作者：
KAMMLER, M;SCHON, C;HANTKE, K
大肠杆菌有一个铁（II）运输系统（feo），这可能对厌氧条件下细胞的铁供应做出重要贡献。铁（II）转运基因的克隆和测序揭示了一个开放的阅读框架（feoA）可能编码一个小蛋白与75个氨基酸和膜蛋白与773个氨基酸（feoB）。feoAB的上游区域含有调节蛋白Fur的结合位点，Fur在所有已知的E.杆菌此外，在启动子区中鉴定了Fnr结合位点。FeoB蛋白在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中的表观分子量为70 kDa，定位于细胞质膜。该序列揭示了与ATP酶同源的区域，这表明亚铁的摄取可能是ATP驱动的。FeoA或FeoB突变体可分别由具有feoA或feoB基因的克隆互补。
Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. Cloning and sequencing of the iron(II) transport genes revealed an open reading frame (feoA) possibly coding for a small protein with 75 amino acids and a membrane protein with 773 amino acids (feoB). The upstream region of feoAB contained a binding site for the regulatory protein Fur, which acts with iron(II) as a corepressor in all known iron transport systems of E. coli. In addition, a Fnr binding site was identified in the promoter region. The FeoB protein had an apparent molecular mass of 70 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and was localized in the cytoplasmic membrane. The sequence revealed regions of homology to ATPases, which indicates that ferrous iron uptake may be ATP driven. FeoA or FeoB mutants could be complemented by clones with the feoA or feoB gene, respectively.