The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms
The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms
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DOI：
10.1099/mic.0.27476-0
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发表时间：
2005-05-01
期刊：
影响因子：
2.8
通讯作者：
Bonnefoy, V
中科院分区：
文献类型：
--
作者：
Bruscella, P;Cassagnaud, L;Bonnefoy, V
从严格嗜酸和化能自养的嗜酸氧化亚铁硫杆菌ATCC 33020中克隆了一个编码高电位铁硫蛋白（HiPIP）的基因，并进行了序列测定。这种潜在的HiPIP在嗜中性和异养大肠杆菌的周质中过量产生。如光学和EPR光谱以及电化学研究所示，重组蛋白具有HiPIP的所有生化性质，表明铁硫簇被正确插入。在Delta tatC突变体中未检测到这种蛋白质在大肠杆菌周质中的易位，表明它依赖于达特系统。菌株ATCC 23270和ATCC 33020中iro基因座的遗传组织与菌株Fe-1和BRGM中发现的不同。事实上，在A.在氧化亚铁杆菌ATCC 33020和ATCC 23270（模式菌株）中，iro不位于purA的下游，而是位于petC 2的下游，petC 2编码来自第二个A的细胞色素c（1）。氧化亚铁细胞色素bc（1）复合物。这些发现强调了A. ferrooxidans物种。结果表明，Iro将电子从细胞色素bc（1）复合物转移到末端氧化酶，正如光合细菌中的HiPIP所提出的那样。
The gene encoding a putative high-potential iron-sulfur protein (HiPIP) from the strictly acidophilic and chemolithoautotrophic Acidithiobacillus ferrooxidans ATCC 33020 has been cloned and sequenced. This potential HiPIP was overproduced in the periplasm of the neutrophile and heterotroph Escherichia coli. As shown by optical and EPR spectra and by electrochemical studies, the recombinant protein has all the biochemical properties of a HiPIP, indicating that the iron-sulfur cluster was correctly inserted. Translocation of this protein in the periplasm of E coli was not detected in a Delta tatC mutant, indicating that it is dependent on the Tat system. The genetic organization of the iro locus in strains ATCC 23270 and ATCC 33020 is different from that found in strains Fe-1 and BRGM. Indeed, in A. ferrooxidans ATCC 33020 and ATCC 23270 (the type strain), iro was not located downstream from purA but was instead downstream from petC2, encoding cytochrome c(1) from the second A. ferrooxidans cytochrome bc(1), complex. These findings underline the genotypic heterogeneity within the A. ferrooxidans species. The results suggest that Iro transfers electrons from a cytochrome bc(1), complex to a terminal oxidase, as proposed for the HiPIP in photosynthetic bacteria.