ZraP, the most prominent zinc protein under zinc stress conditions has no direct role in in-vivo zinc tolerance in Escherichia coli.

Autor: van der Weel L; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., As KS; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., Dekker WJC; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., van den Eijnden L; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., van Helmond W; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., Schiphorst C; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., Hagen WR; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., Hagedoorn PL; Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands. Electronic address: p.l.hagedoorn@tudelft.nl.
Jazyk: angličtina
Zdroj: Journal of inorganic biochemistry [J Inorg Biochem] 2019 Mar; Vol. 192, pp. 98-106. Date of Electronic Publication: 2018 Dec 27.
DOI: 10.1016/j.jinorgbio.2018.12.013
Abstrakt: Escherichia coli ZraP (zinc resistance associated protein) is the major Zn containing soluble protein under Zn stress conditions. ZraP is the accessory protein of a bacterial two-component, Zn 2+ sensitive signal transduction system ZraSR. ZraP has also been reported to act as a Zn 2+ dependent molecular chaperone. An explanation why ZraP is the major Zn protein under the stress condition of Zn 2+ overload (0.2 mM) has remained elusive. We have recombinantly produced E. coli ZraP and measured Zn 2+ and Cu 2+ affinity in-vitro using Isothermal Titration Calorimetry. ZraP has a significantly higher affinity for Cu 2+ than for Zn 2+ . Mutation of the conserved Cys 102 to Ala or Ser resulted in a change of the oligomeric state of the protein. Mutation of the conserved His 107 to Ala did not affect the zinc binding affinity or the oligomeric state of the protein. Deletion of the ZraP coding gene from the E. coli genome resulted in a phenotype with tolerance to very high zinc concentrations (up to 2.5 mM) that were lethal to wild type E. coli. These results exclude a direct role for ZraP in Zn 2+ tolerance in E. coli.
(Copyright © 2018 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: