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Title: Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and mercury by ZinT

Journal Article · · Biochemical and Biophysical Research Communications
;  [1]
  1. School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT (United Kingdom)

ZinT (B1973), previously known as YodA, was originally characterised as a cadmium-induced periplasmic protein under the regulation of Fur and SoxS. Here we describe a decrease in zinT transcript in response to elevated copper concentrations and the zinc and copper dependent phenotype of a {delta}zinT strain. Cadmium sensitivity of the {delta}zinT strain was not observed. We demonstrate the binding of nickel, zinc, cadmium, and mercury, but not cobalt, copper, iron, and manganese, to purified ZinT using mass spectrometry. This and previous studies support the hypothesis that ZinT plays a role in zinc homeostasis and is required for growth under zinc limited conditions, suggesting that ZinT is either a periplasmic zinc chaperone or is involved in zinc import. Limited metal ion discrimination results in regulation of PzinT in a non-specific manner, which is mirrored in the binding of several different heavy metals by ZinT.

OSTI ID:
21033000
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 364, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2007.09.094; PII: S0006-291X(07)02090-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English

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