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Issue 4, 2015
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Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator

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Abstract

Staphylococcus aureus possesses two canonical ABC-importers dedicated to nickel acquisition: the NikABCDE and the CntABCDF systems, active under different growth conditions. This study reports on the extracytoplasmic nickel-binding components SaNikA and SaCntA. We showed by protein crystallography that SaNikA is able to bind either a Ni-(L-His)2 complex or a Ni-(L-His) (2-methyl-thiazolidine dicarboxylate) complex, depending on their availability in culture supernatants. Native mass spectrometry experiments on SaCntA revealed that it binds the Ni(II) ion via a different histidine-dependent chelator but it cannot bind Ni-(L-His)2. In vitro experiments are consistent with in vivo nickel content measurements that showed that L-histidine has a high positive impact on nickel import via the Cnt system. These results suggest that although both systems may require free histidine, they use different strategies to import nickel.

Graphical abstract: Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator

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Publication details

The article was received on 12 Nov 2014, accepted on 13 Jan 2015 and first published on 14 Jan 2015


Article type: Paper
DOI: 10.1039/C4MT00295D
Metallomics, 2015,7, 613-621

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    Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator

    H. Lebrette, E. Borezée-Durant, L. Martin, P. Richaud, E. Boeri Erba and C. Cavazza, Metallomics, 2015, 7, 613
    DOI: 10.1039/C4MT00295D

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