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

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.
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Article dans une revue
Metallomics : integrated biometal science, 2015, 7 (4), pp.613-21
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http://hal.univ-grenoble-alpes.fr/hal-01149525
Contributeur : Frank Thomas <>
Soumis le : jeudi 7 mai 2015 - 11:24:24
Dernière modification le : jeudi 11 janvier 2018 - 06:21:13

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  • HAL Id : hal-01149525, version 1
  • PUBMED : 25611161

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Hugo Lebrette, E Borezée-Durant, Lydie Martin, P Richaud, Elisabetta Boeri Erba, et al.. Novel insights into nickel import in Staphylococcus aureus: the positive role of free histidine and structural characterization of a new thiazolidine-type nickel chelator.. Metallomics : integrated biometal science, 2015, 7 (4), pp.613-21. 〈hal-01149525〉

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