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Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein

Aviv Meir, Gulshan Walke, Fabian Schwerdtfeger, Lada Gevorkyan-Airapetov, View ORCID ProfileSharon Ruthstein
doi: https://doi.org/10.1101/681486
Aviv Meir
1Department of Chemistry; Bar-Ilan University, Ramat Gan, 5290002, Israel
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Gulshan Walke
1Department of Chemistry; Bar-Ilan University, Ramat Gan, 5290002, Israel
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Fabian Schwerdtfeger
1Department of Chemistry; Bar-Ilan University, Ramat Gan, 5290002, Israel
2Department of Chemistry and Pharmacy, Albert-Ludwigs-University, Freiburg, 79085 Germany
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Lada Gevorkyan-Airapetov
1Department of Chemistry; Bar-Ilan University, Ramat Gan, 5290002, Israel
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Sharon Ruthstein
1Department of Chemistry; Bar-Ilan University, Ramat Gan, 5290002, Israel
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  • ORCID record for Sharon Ruthstein
  • For correspondence: Sharon.ruthstein@biu.ac.il
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Abstract

The dissemination of resistant pathogenic microbes has become one of the most challenging problems that modern medicine has faced. Developing novel drugs based on new molecular targets that previously were not targeted, is therefore the highest priority in antibiotics research. One approach that has been recently suggested is to inhibit copper transporters in prokaryotic systems. Copper is required for many biological pathways, but sometimes it can harm the cell. Pathogenic systems have a highly sophisticated copper-regulation network; therefore, a better understanding of how this network operates at the molecular level should assist in developing the next generation of antibiotics. The CusB protein is part of the CusCBA periplasmic Cu(I) efflux system in Gram-negative bacteria, and it was recently reported to play a key role in the functioning of the whole CusCBA system, in which conformational changes as well as the assembly/disassembly process control the opening of the transporter. More knowledge of the underlying mechanism is needed to attain a full understanding of CusB functioning, which is associated with targeting specific and crucial residues in CusB. Here, we combine in-vitro structural measurements, which used EPR spectroscopy and UV-Vis measurements, with cell experiments to explore the role of the various methionine residues in CusB. We targeted two methionine residues (M227 and M241) that are essential for the proper function of CusB.

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  • Conflicts of Interest: The authors declare no conflict of interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted June 24, 2019.
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Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein
Aviv Meir, Gulshan Walke, Fabian Schwerdtfeger, Lada Gevorkyan-Airapetov, Sharon Ruthstein
bioRxiv 681486; doi: https://doi.org/10.1101/681486
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Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein
Aviv Meir, Gulshan Walke, Fabian Schwerdtfeger, Lada Gevorkyan-Airapetov, Sharon Ruthstein
bioRxiv 681486; doi: https://doi.org/10.1101/681486

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