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J. Biol. Chem., Vol. 280, Issue 37, 32254-32261, September 16, 2005

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A Bacterial Glutathione Transporter (Escherichia coli CydDC) Exports Reductant to the Periplasm^*

From the Department of Molecular Biology and Biotechnology, Firth Court, The University of Sheffield, Sheffield S10 2TN, United Kingdom

Glutathione (GSH), a major biological antioxidant, maintains redox balance in prokaryotes and eukaryotic cells and forms exportable conjugates with compounds of pharmacological and agronomic importance. However, no GSH transporter has been characterized in a prokaryote. We show here that a heterodimeric ATP-binding cassette-type transporter, CydDC, mediates GSH transport across the Escherichia coli cytoplasmic membrane. In everted membrane vesicles, GSH is imported via an ATP-driven, protonophore-insensitive, orthovanadate-sensitive mechanism, equating with export to the periplasm in intact cells. GSH transport and cytochrome bd quinol oxidase assembly are abolished in the cydD1 mutant. Glutathione disulfide (GSSG) was not transported in either Cyd⁺ or Cyd^– strains. Exogenous GSH restores defective swarming motility and benzylpenicillin sensitivity in a cydD mutant and also benzylpenicillin sensitivity in a gshA mutant defective in GSH synthesis. Overexpression of the cydDC operon in dsbD mutants defective in disulfide bond formation restores dithiothreitol tolerance and periplasmic cytochrome b assembly, revealing redundant pathways for reductant export to the periplasm. These results identify the first prokaryotic GSH transporter and indicate a key role for GSH in periplasmic redox homeostasis.

Received for publication, March 21, 2005 , and in revised form, July 19, 2005.

^* This work was supported by Biotechnology and Biological Sciences Research CouncilGrant 50/P12980 (to R. K. P.) and a University of Sheffield White Rose Studentship (to H. C. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 44-114-222-4447; Fax: 44-114-222-2800; E-mail: r.poole{at}sheffield.ac.uk.

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