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

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@article{94ce4c222041443f98095681697d5a28,
title = "Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and mercury by ZinT.",
abstract = "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 DeltazinT strain. Cadmium sensitivity of the DeltazinT 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.",
keywords = "ZinT, zinc import, cadmium, YodA, mercury",
author = "CJ Kershaw and Nigel Brown and Jonathan Hobman",
year = "2007",
month = dec,
day = "7",
doi = "10.1016/j.bbrc.2007.09.094",
language = "English",
volume = "364",
pages = "66--71",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and mercury by ZinT.

AU - Kershaw, CJ

AU - Brown, Nigel

AU - Hobman, Jonathan

PY - 2007/12/7

Y1 - 2007/12/7

N2 - 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 DeltazinT strain. Cadmium sensitivity of the DeltazinT 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.

AB - 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 DeltazinT strain. Cadmium sensitivity of the DeltazinT 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.

KW - ZinT

KW - zinc import

KW - cadmium

KW - YodA

KW - mercury

U2 - 10.1016/j.bbrc.2007.09.094

DO - 10.1016/j.bbrc.2007.09.094

M3 - Article

C2 - 17931600

VL - 364

SP - 66

EP - 71

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -