c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm.

作者: Anne Durand , Asma Azzouzi , Marie-Line Bourbon , Anne-Soisig Steunou , Sylviane Liotenberg

DOI: 10.1128/MBIO.01007-15

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摘要: ABSTRACT In the absence of a tight control copper entrance into cells, bacteria have evolved different systems to concentration within cytoplasm and periplasm. Central these systems, Cu + ATPase CopA plays major role in tolerance translocates from The fate periplasm varies among species. Copper can be sequestered, oxidized, or released outside cells. Here we describe identification CopI, periplasmic protein present many proteobacteria, show its requirement for Rubrivivax gelatinosus. Δ copI mutant is more susceptible than copA mutant. CopI induced by copper, localized could bind copper. Interestingly, affects cytochrome c membrane complexes ( cbb 3 oxidase photosystem) both -null mutants, but causes are different. mutant, heme chlorophyll synthesis affected, whereas decrease consequence impaired assembly. This impact on -type cytochromes would contribute also toxicity wild-type cells when they exposed high concentrations. IMPORTANCE an essential cation required as cofactor enzymes involved vital processes such respiration, photosynthesis, free radical scavenging, pathogenesis. However, highly toxic has been implicated disorders all organisms, including humans, because it catalyze production reactive oxygen species targets various biosynthesis pathways. Identifying targets, provides insights homeostatic mechanisms tolerance. this work, first time direct effect excess We that specifically , thus suggesting biogenesis.

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