Discovery and characterization of UipA, a uranium- and iron-binding PepSY protein involved in uranium tolerance by soil bacteria View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2021-09-23

AUTHORS

Nicolas Gallois, Béatrice Alpha-Bazin, Nicolas Bremond, Philippe Ortet, Mohamed Barakat, Laurie Piette, Abbas Mohamad Ali, David Lemaire, Pierre Legrand, Nicolas Theodorakopoulos, Magali Floriani, Laureline Février, Christophe Den Auwer, Pascal Arnoux, Catherine Berthomieu, Jean Armengaud, Virginie Chapon

ABSTRACT

Uranium is a naturally occurring radionuclide. Its redistribution, primarily due to human activities, can have adverse effects on human and non-human biota, which poses environmental concerns. The molecular mechanisms of uranium tolerance and the cellular response induced by uranium exposure in bacteria are not yet fully understood. Here, we carried out a comparative analysis of four actinobacterial strains isolated from metal and radionuclide-rich soils that display contrasted uranium tolerance phenotypes. Comparative proteogenomics showed that uranyl exposure affects 39–47% of the total proteins, with an impact on phosphate and iron metabolisms and membrane proteins. This approach highlighted a protein of unknown function, named UipA, that is specific to the uranium-tolerant strains and that had the highest positive fold-change upon uranium exposure. UipA is a single-pass transmembrane protein and its large C-terminal soluble domain displayed a specific, nanomolar binding affinity for UO22+ and Fe3+. ATR-FTIR and XAS-spectroscopy showed that mono and bidentate carboxylate groups of the protein coordinated both metals. The crystal structure of UipA, solved in its apo state and bound to uranium, revealed a tandem of PepSY domains in a swapped dimer, with a negatively charged face where uranium is bound through a set of conserved residues. This work reveals the importance of UipA and its PepSY domains in metal binding and radionuclide tolerance. More... »

PAGES

705-716

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41396-021-01113-7

DOI

http://dx.doi.org/10.1038/s41396-021-01113-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1141322181

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/34556817


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