Bacterial cells require copper for several important enzymes such as superoxide dismutase and cytochrome c oxidase. However, when copper concentration is highly regulated, it leads to the bacteria’s death. Understanding the copper regulation mechanism in bacteria is essential for two reasons: first, the copper regulation system in bacteria is intriguing, and much more complex than in eukaryotic cells. Copper regulation in bacteria involves various membrane transporters, protein-DNA complexes and metallochaperones, thus, resolving the copper cycle in prokaryotic systems will shed light on the function of these unique biological systems. Second, copper has been used throughout much of the human civilization as an antimicrobial agent. Hence, a detailed understanding of the copper resistance mechanism in bacteria is vital both to identify the microorganisms’ degree of survival in the mammalian cell, and for the development of new antibiotics.
Selected publications:
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Yasin, A.; Mandato, A.; Hofmann, L.; Igbaria-Jaber, Y.; Shenberger, Y.; Gevorkyan-Airapetov, L.; Saxena, S.; Ruthstein, S.; The dynamic plasticity of P. aerguinosa CueR copper transcription factor upon cofactor and DNA binding. ChemBioChem. 2024, e202400279
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Igbaria-Jaber, Y.; Hofmann, L.; Gevorkyan-Airapetov, L.; Shenberger, Y.; Ruthstein, S.; Revealing the DNA binding modes of CsoR by EPR spectroscopy. ACS Omega. 2023, 8, 39886-39895.
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Shenberger, Y.; Gevorkyan-Airapetov, L.; Hirsch, M.; Hofmann, L.;Ruthstein, S.; An in-cell spin-labelling methodology provides structural information on cytoplasmic proteins in bacteria. Chem. Comm. 2023, 59. 10524-10527.
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Hofmann, L.; Mandato, A.; Saxena, S.; Ruthstein, S.; The use of EPR sepctroscopy to study transcription mechanisms. Biophys. Rev. 2022, 14, 1141-1159.
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Yakobov, I.; Mandato, A.; Hofmann, L.; Singewald, K.; Shenberger, Y.; Gevorkyan-Airapetov, L.; Saxena, S.; Ruthstein, S.; Allostery-driven changes in dynamics regulate the activation of bacterial copper transcription factor. Protein. Sci. 2022, 31, e4309
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Meir, A.; Abdelhai, A.; Moskovitz, Y.; Ruthstein, S.; EPR spectroscopy targets conformational and topological changes in the E.coli membrane fusion CusB dimer upon Cu(I) binding. Biophys. J. 2017, 112, 2494-250