Metal‐responsive RNA polymerase extracytoplasmic function (ECF) sigma factors

In order to survive, bacteria must adapt to multiple fluctuations in their environment, including coping with changes in metal concentrations. Many metals are essential for viability, since they act as cofactors of indispensable enzymes. But on the other hand, they are potentially toxic because they generate reactive oxygen species or displace other metals from proteins, turning them inactive. This dual effect of metals forces cells to maintain homeostasis using a variety of systems to import and export them. These systems are usually inducible, and their expression is regulated by metal sensors and signal‐transduction mechanisms, one of which is mediated by extracytoplasmic function (ECF) sigma factors. In this review, we have focused on the metal‐responsive ECF sigma factors, several of which are activated by iron depletion (FecI, FpvI and PvdS), while others are activated by excess of metals such as nickel and cobalt (CnrH), copper (CarQ and CorE) or cadmium and zinc (CorE2). We focus particularly on their physiological roles, mechanisms of action and signal transduction pathways.     

The chromosomally encoded cation diffusion facilitator proteins DmeF and FieF from Wautersia metallidurans CH34 are transporters of broad metal specificity

Genomic sequencing of the beta-proteobacterium Wautersia (previously Ralstonia) metallidurans CH34 revealed the presence of three genes encoding proteins of the cation diffusion facilitator (CDF) family. One, CzcD, was previously found to be part of the high-level metal resistance system Czc that mediates the efflux of Co(II), Zn(II), and Cd(II) ions catalyzed by the CzcCBA cation-proton antiporter. The second CDF protein, FieF, is probably mainly a ferrous iron detoxifying protein but also mediated some resistance against other divalent metal cations such as Zn(II), Co(II), Cd(II), and Ni(II) in W. metallidurans or Escherichia coli. The third CDF protein, DmeF, showed the same substrate spectrum as FieF, but with different preferences. DmeF plays the central role in cobalt homeostasis in W. metallidurans, and a disruption of dmeF rendered the high-level metal cation resistance systems Czc and Cnr ineffective against Co(II). This is evidence for the periplasmic detoxification of substrates by RND transporters of the heavy metal efflux family subgroup.     

部分革兰氏阴性菌胞外功能 sigma因子结构与调控铁离子的利用机制

铁离子是大多数细菌生存所必需的一种营养物质,但摄入过多的铁离子也会对细菌造成损伤。因此,细菌对铁离子的摄取受到严格调控。革兰氏阴性菌对铁离子的摄取主要受Fur (ferric uptake regulator) 蛋白和σ（sigma）因子的调控。σ因子是RNA聚合酶的可解离亚基,能使RNA聚合酶结合到基因的启动子区域,从而引起基因转录。因此,σ因子在原核生物转录起始过程中必不可少。细菌中存在多种σ因子,参与铁离子调控的σ因子即是胞外功能σ因子（extra cytoplasmic function sigma factor, ECF sigma factor）。通常,胞外功能σ因子活性可被抗σ因子（anti sigma factor）抑制。当受到外界环境信号的刺激,σ因子与抗σ因子解离,从而使σ因子活化并结合RNA聚合酶核心酶形成全酶,引起目的基因的转录。本文将就胞外功能σ因子在σ因子家族中的分类地位、结构特点以及对3价铁离子和血红素的转运调控机制作一综述。