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Cytosolic Copper Binding by a Bacterial Storage Protein and Interplay with Copper Efflux

Lookup NU author(s): Jaeick Lee, Professor Christopher Dennison



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Escherichia coli has a well-characterized copper (Cu) transporting ATPase (CopA) that removes this potentially toxic metal ion from the cytosol. Growth of the strain lacking CopA (ΔcopA) is inhibited above 0.5 mM Cu, whilst a similar effect does not occur in wild type (WT) E. coli until over 2.5 mM Cu. Limited expression of CopA can restore growth to WT levels in ΔcopAE. coli in the presence of Cu. To study the influence of a bacterial cytosolic Cu storage protein (Csp3) on how E. coli handles Cu, the protein from Bacillus subtilis (BsCsp3) has been expressed in the WT and ΔcopA strains. BsCsp3 can protect both strains from Cu toxicity, promoting growth at up to ~1.5 and ~3.5 mM Cu, respectively. Higher levels of Csp3 expression are needed to provide resistance to Cu toxicity in ΔcopAE. coli. At 1.5 mM Cu, BsCsp3 purified from ΔcopAE. coli binds up to approximately four equivalents of Cu(I) per monomer. A similar number of Cu(I) equivalents can be bound by BsCsp3 purified from WT E. coli also grown at 1.5 mM Cu, a concentration that does not cause toxicity in this strain. Much lower amounts of BsCsp3 are produced in WT E. coli grown in the presence of 3.4 mM Cu, but the protein still counteracts toxicity and is almost half loaded with Cu(I). Csp3s can protect E. coli from Cu toxicity by sequestering cuprous ions in the cytosol. This appears to include an ability to acquire and withhold Cu(I) from the main efflux system in a heterologous host.

Publication metadata

Author(s): Lee J, Dennison C

Publication type: Article

Publication status: Published

Journal: International journal of Molecular Sciences

Year: 2019

Volume: 20

Issue: 17

Online publication date: 25/08/2019

Acceptance date: 12/08/2019

Date deposited: 18/09/2019

ISSN (print): 1661-6596

ISSN (electronic): 1422-0067

Publisher: MDPI AG


DOI: 10.3390/ijms20174144

PubMed id: 31450649


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