Santos, Sandra P.Yang, YangRosa, Margarida T.G.Rodrigues, Mafalda A.A.De La Tour, Claire BouthierSommer, SuzanneTeixeira, MiguelCarrondo, Maria A.Cloetens, PeterAbreu, Isabel A.Romão, Célia V.2020-01-232020-01-232019-12-012045-2322PURE: 15763358PURE UUID: 67da4eb3-c17c-41ad-a9a9-329ef1b6a618Scopus: 85075342637PubMed: 31748604ORCID: /0000-0003-4124-6237/work/67534115http://hdl.handle.net/10362/91695The bacterium Deinococcus radiodurans is highly resistant to several stress conditions, such as radiation. According to several reports, manganese plays a crucial role in stress protection, and a high Mn/Fe ratio is essential in this process. However, mobilization of manganese and iron, and the role of DNA-binding-proteins-under-starved-conditions during oxidative-stress remained open questions. We used synchrotron-based X-ray fluorescence imaging at nano-resolution to follow element-relocalization upon stress, and its dependency on the presence of Dps proteins, using dps knockout mutants. We show that manganese, calcium, and phosphorus are mobilized from rich-element regions that resemble electron-dense granules towards the cytosol and the cellular membrane, in a Dps-dependent way. Moreover, iron delocalizes from the septum region to the cytoplasm affecting cell division, specifically in the septum formation. These mechanisms are orchestrated by Dps1 and Dps2, which play a crucial role in metal homeostasis, and are associated with the D. radiodurans tolerance against reactive oxygen species.2999442engGeneraljournal article10.1038/s41598-019-53140-2https://www.scopus.com/pages/publications/85075342637https://www.nature.com/articles/s41598-019-53140-2