Affiliation:
1. Institute for Biology
2. Institute for Biochemistry/Biotechnology, Life Science Faculty, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3, 06099 Halle, Germany
Abstract
ABSTRACT
Glutathione (GSH) and its derivative phytochelatin are important binding factors in transition-metal homeostasis in many eukaryotes. Here, we demonstrate that GSH is also involved in chromate, Zn(II), Cd(II), and Cu(II) homeostasis and resistance in
Escherichia coli
. While the loss of the ability to synthesize GSH influenced metal tolerance in wild-type cells only slightly, GSH was important for residual metal resistance in cells without metal efflux systems. In mutant cells without the P-type ATPase ZntA, the additional deletion of the GSH biosynthesis system led to a strong decrease in resistance to Cd(II) and Zn(II). Likewise, in mutant cells without the P-type ATPase CopA, the removal of GSH led to a strong decrease of Cu(II) resistance. The precursor of GSH, γ-glutamylcysteine (γEC), was not able to compensate for a lack of GSH. On the contrary, γEC-containing cells were less copper and cadmium tolerant than cells that contained neither γEC nor GSH. Thus, GSH may play an important role in trace-element metabolism not only in higher organisms but also in bacteria.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
178 articles.
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