Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2013 Dec;29(6):397-405.
doi: 10.1007/s10565-013-9262-1. Epub 2013 Sep 27.

Molecular basis of active copper resistance mechanisms in Gram-negative bacteria

Kinga Bondarczuk  1 , Zofia Piotrowska-Seget
Affiliations
Review

Molecular basis of active copper resistance mechanisms in Gram-negative bacteria

Kinga Bondarczuk et al. Cell Biol Toxicol. 2013 Dec.

Abstract

Copper is a metallic element that is crucial for cell metabolism; however, in extended concentrations, it is toxic for all living organisms. The dual nature of copper has forced organisms, including bacteria, to keep a tight hold on cellular copper content. This challenge has led to the evolution of complex mechanisms that on one hand enable them to deliver the essential element and on the other to protect cells against its toxicity. Such mechanisms have been found in both eukaryotic and prokaryotic cells. In bacteria a number of different systems such as extra- and intracellular sequestration, enzymatic detoxification, and metal removal from the cell enabling them to survive in the presence of high concentration of copper have been identified. Gram-negative bacteria, due to their additional compartment, need to deal with both cytoplasmic and periplasmic copper. Therefore, these bacteria have evolved intricate and precisely regulated systems which interact with each other. In this review the active mechanisms of copper resistance at their molecular level are discussed.

PubMed Disclaimer

Figures

Fig. 1
Fig. 1
Proteins involved in copper resistance in bacteria. Abbreviations: CM cytoplasmic membrane, PS periplasmic space, OM outer membrane. Assignment of particular proteins: multicopper oxidase (CueO), RND (CusA), MFP (CusB), OMF (CusC), copper chaperone (CusF), ATPase (CopA)
Fig. 2
Fig. 2
A model for cop system in P. syringae pv. Tomato. Abbreviations: CM cytoplasmic membrane, PS periplasmic space, OM outer membrane. Arrows indicate presumed interactions between proteins (modified from Puig et al. 2002)
See this image and copyright information in PMC

References

    1. Arnesano F, Banci L, Bertini I, Thompsett AR. Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasis. Structure. 2002;10:1337–1347. doi: 10.1016/S0969-2126(02)00858-4. - DOI - PubMed
    1. Bagai I, Liu W, Rensing C, Blackburn NJ, McEvoy MM. Substrate-linked conformational change in the periplasmic component of Cu(I)/Ag (I) efflux system. J Biol Chem. 2007;282:35695–35702. doi: 10.1074/jbc.M703937200. - DOI - PubMed
    1. Bagai I, Rensing C, Blackburn NJ, McEvoy MM. Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry. 2008;47:11408–11414. doi: 10.1021/bi801638m. - DOI - PMC - PubMed
    1. Bannister JV, Bannister WH. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit Rev Biochem. 1987;22:111–190. doi: 10.3109/10409238709083738. - DOI - PubMed
    1. Cha JS, Cooksey DA. Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Microbiology. 1991;88:8915–8919. - PMC - PubMed

MeSH terms

LinkOut - more resources