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• W2977783892 abstract "Copper and iron are trace elements that form an indispensable part of many proteins and are crucial for the well-being of all cells. At the same time, the intracellular levels of these metals require careful regulation, as excess or deficiency may be lethal. P1B-ATPases are key players in metal homeostasis. They belong to the superfamily of P-type ATPases, transmembrane proteins present in virtually all life forms, are responsible for solute translocation across biological membranes. The goal of this thesis is to improve our understanding of the structural and functional roles of P1B-ATPases in metal homeostasis by focusing on the host-microbe interaction. The thesis first describes the importance of Cu+ distribution in the outcome of host-microbe interaction. Copper is an important element in host–microbe interactions, acting both as a catalyst in enzymes and as a potential toxin. Cu+-ATPases drive cytoplasmic Cu+ efflux and protect bacteria against metal overload. Many pathogenic and symbiotic bacteria contain multiple Cu+-ATPase genes within particular genetic environments, suggesting alternative roles for each resulting protein. This hypothesis was tested by characterizing five homologous Cu+-ATPases present in the symbiotic organism Sinorhizobium meliloti. Mutation of each gene led to different phenotypes and abnormal nodule development in the alfalfa host. Distinct responses were detected in free-living S. meliloti mutant strains exposed to metal and redox stresses. Differential gene expression was detected under Cu+, oxygen or nitrosative stress. These observations suggest that CopA1a maintains the cytoplasmic Cu+ quota and its expression is controlled by Cu+ levels. CopA1b is also regulated by Cu+ concentrations and is required during symbiosis for bacteroid maturation. CopA2-like proteins, FixI1 and FixI2, are necessary for the assembly of two different cytochrome c oxidases at different stages of bacterial life. CopA3 is a phylogenetically distinct Cu+-ATPase that does not contribute to Cu+ tolerance. It is regulated by redox stress and required during symbiosis. We postulated a model where non-redundant homologous Cu+-ATPases, operating under distinct regulation, transport Cu+ to different target proteins. In its second part, the thesis describes the novel Fe2+-ATPases and their influence in the host-microbe interaction. Little is known about iron efflux transporters in bacterial systems. Recently, the participation of Bacillus subtilis PfeT, a P1B4-ATPase, in cytoplasmic Fe2+ efflux has been proposed. We report here the distinct roles of mycobacterial P1B4-ATPases in the homeostasis of Co2+ and Fe2+. Mutation of Mycobacterium smegmatis ctpJ affects the homeostasis of both ions. Alternatively, a M. tuberculosis ctpJ…" @default.
• W2977783892 created "2019-10-10" @default.
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• W2977783892 date "2016-04-04" @default.
• W2977783892 modified "2023-09-26" @default.
• W2977783892 title "Functional Diversity of Homologous P1B-ATPases in Metal Homeostasis and Host-Microbe Interaction" @default.
• W2977783892 hasPublicationYear "2016" @default.
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