The metal permease ZupT from Escherichia coli is a transporter with a broad substrate spectrum.

Abstract:

:The Escherichia coli zupT (formerly ygiE) gene encodes a cytoplasmic membrane protein (ZupT) related to members of the eukaryotic ZIP family of divalent metal ion transporters. Previously, ZupT was shown to be responsible for uptake of zinc. In this study, we show that ZupT is a divalent metal cation transporter of broad substrate specificity. An E. coli strain with a disruption in all known iron uptake systems could grow in the presence of chelators only if zupT was expressed. Heterologous expression of Arabidopsis thaliana ZIP1 could also alleviate iron deficiency in this E. coli strain, as could expression of indigenous mntH or feoABC. Transport studies with intact cells showed that ZupT facilitates uptake of 55Fe2+ similarly to uptake of MntH or Feo. Other divalent cations were also taken up by ZupT, as shown using 57Co2+. Expression of zupT rendered E. coli cells hypersensitive to Co2+ and sensitive to Mn2+. ZupT did not appear to be metal regulated: expression of a Phi(zupT-lacZ) operon fusion indicated that zupT is expressed constitutively at a low level.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Grass G,Franke S,Taudte N,Nies DH,Kucharski LM,Maguire ME,Rensing C

doi

10.1128/JB.187.5.1604-1611.2005

keywords:

subject

Has Abstract

pub_date

2005-03-01 00:00:00

pages

1604-11

issue

5

eissn

0021-9193

issn

1098-5530

pii

187/5/1604

journal_volume

187

pub_type

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