Straw, Megan L and Chaplin, Amanda K and Hough, Michael A and Paps, Jordi and Bavro, Vassiliy N and Wilson, Michael T and Vijgenboom, Erik and Worrall, Jonathan AR (2018) A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans. Metallomics: integrated biometal science, 2018 (10). pp. 180-193. DOI https://doi.org/10.1039/c7mt00299h
Straw, Megan L and Chaplin, Amanda K and Hough, Michael A and Paps, Jordi and Bavro, Vassiliy N and Wilson, Michael T and Vijgenboom, Erik and Worrall, Jonathan AR (2018) A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans. Metallomics: integrated biometal science, 2018 (10). pp. 180-193. DOI https://doi.org/10.1039/c7mt00299h
Straw, Megan L and Chaplin, Amanda K and Hough, Michael A and Paps, Jordi and Bavro, Vassiliy N and Wilson, Michael T and Vijgenboom, Erik and Worrall, Jonathan AR (2018) A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans. Metallomics: integrated biometal science, 2018 (10). pp. 180-193. DOI https://doi.org/10.1039/c7mt00299h
Abstract
Streptomyces lividans has a distinct dependence on the bioavailability of copper for its morphological development. A cytosolic copper resistance system is operative in S. lividans that serves to preclude deleterious copper levels. This system comprises of several CopZ-like copper chaperones and P1-type ATPases, predominantly under the transcriptional control of a metalloregulator from the copper sensitive operon repressor (CsoR) family. In the present study, we discover a new layer of cytosolic copper resistance in S. lividans that involves a protein belonging to the newly discovered family of copper storage proteins, which we have named Ccsp (cytosolic copper storage protein). From an evolutionary perspective, we find Ccsp homologues to be widespread in Bacteria and extend through into Archaea and Eukaryota. Under copper stress Ccsp is upregulated and consists of a homotetramer assembly capable of binding up to 80 cuprous ions (20 per protomer). X-ray crystallography reveals 18 cysteines, 3 histidines and 1 aspartate are involved in cuprous ion coordination. Loading of cuprous ions to Ccsp is a cooperative process with a Hill coefficient of 1.9 and a CopZ-like copper chaperone can transfer copper to Ccsp. A Δccsp mutant strain indicates that Ccsp is not required under initial copper stress in S. lividans, but as the CsoR/CopZ/ATPase efflux system becomes saturated, Ccsp facilitates a second level of copper tolerance.
Item Type: | Article |
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Uncontrolled Keywords: | Cytosol; Streptomyces lividans; Copper; Bacterial Proteins; Crystallography, X-Ray; Cloning, Molecular; Protein Conformation; Protein Binding; Operon; Metallochaperones |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 31 Jul 2019 13:08 |
Last Modified: | 30 Oct 2024 15:54 |
URI: | http://repository.essex.ac.uk/id/eprint/24509 |
Available files
Filename: notes_final_3 copy.pdf