Abstract:
: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, Zn2+ sensitive signal transduction system ZraSR. ZraP has also been reported to act as a Zn2+ dependent molecular chaperone. An explanation why ZraP is the major Zn protein under the stress condition of Zn2+ overload (0.2 mM) has remained elusive. We have recombinantly produced E. coli ZraP and measured Zn2+ and Cu2+ affinity in-vitro using Isothermal Titration Calorimetry. ZraP has a significantly higher affinity for Cu2+ than for Zn2+. Mutation of the conserved Cys102 to Ala or Ser resulted in a change of the oligomeric state of the protein. Mutation of the conserved His107 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 Zn2+ tolerance in E. coli.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
van der Weel L,As KS,Dekker WJC,van den Eijnden L,van Helmond W,Schiphorst C,Hagen WR,Hagedoorn PLdoi
10.1016/j.jinorgbio.2018.12.013subject
Has Abstractpub_date
2019-03-01 00:00:00pages
98-106eissn
0162-0134issn
1873-3344pii
S0162-0134(18)30574-9journal_volume
192pub_type
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