Cysteine Is Exported from the Escherichia coliCytoplasm by CydDC, an ATP-binding Cassette-type Transporter Required for Cytochrome Assembly

Pittman, Marc S.; Corker, Hazel; Wu, Guanghui; Binet, Marie B.; Moir, Arthur J. G.; Poole, Robert K.

doi:10.1074/jbc.m205615200

Cited by 107 publications

(121 citation statements)

References 65 publications

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“…Benzylpenicillin and Dithiothreitol (DTT)-These were conducted essentially as described before (26) except that DTT sensitivity was measured in disk diffusion assays. Filter-sterilized solutions (10 l) of the stated DTT concentration were pipetted onto sterile filter paper disks (5-mm diameter) that were laid on a lawn of bacteria prepared from an overnight culture.…”

Section: Assays Of Motility and Sensitivity Tomentioning

confidence: 99%

“…Recently, we demonstrated that an ABC-type transporter, CydDC, originally identified by its requirement for assembly of the cytochrome bd-type terminal oxidase of E. coli (23)(24)(25), is a transporter of cysteine outwards across the cytoplasmic membrane (26). Given the established roles of GSH in redox buffering in eukaryotic cells (7), we hypothesized that GSH is also a substrate of CydDC.…”

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confidence: 99%

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

Pittman

Robinson

Poole

2005

Journal of Biological Chemistry

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166

138

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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.

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Section: Assays Of Motility and Sensitivity Tomentioning

confidence: 99%

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confidence: 99%

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

Pittman

Robinson

Poole

2005

Journal of Biological Chemistry

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166

138

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“…2). In Escherichia coli the last two genes are required for the formation of active cytochrome bd (11,27) and encode an ABC transporter which was reported to catalyze the export of L-cysteine (25) and glutathione (26). Since C. glutamicum does not possess a proton-or sodium ion-pumping NADH dehydrogenase, only the cytochrome bc 1 -aa 3 supercomplex and cytochrome bd oxidase couple electron transfer to the generation of an electrochemical proton gradient.…”

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confidence: 99%

Role of Cytochrome bd Oxidase from Corynebacterium glutamicum in Growth and Lysine Production

Kabus

Niebisch

Bott

2007

Appl Environ Microbiol

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Corynebacterium glutamicum possesses two terminal oxidases, cytochrome aa 3 and cytochrome bd. Cytochrome aa 3 forms a supercomplex with the cytochrome bc 1 complex, which contains an unusual diheme cytochrome c 1 . Both the bc 1 -aa 3 supercomplex and cytochrome bd transfer reducing equivalents from menaquinol to oxygen; however, they differ in their proton translocation efficiency by a factor of three. Here, we analyzed the role of cytochrome bd for growth and lysine production. When cultivated in glucose minimal medium, a cydAB deletion mutant of C. glutamicum ATCC 13032 grew like the wild type in the exponential phase, but growth thereafter was inhibited, leading to a biomass formation 40% less than that of the wild type. Constitutive overproduction of functional cytochrome bd oxidase in ATCC 13032 led to a reduction of the growth rate by ϳ45% and of the maximal biomass by ϳ35%, presumably as a consequence of increased electron flow through the inefficient cytochrome bd oxidase. In the L-lysine-producing C. glutamicum strain MH20-22B, deletion of the cydAB genes had only minor effects on growth rate and biomass formation, but lysine production was increased by ϳ12%. Thus, the respiratory chain was shown to be a target for improving amino acid production by C. glutamicum.

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“…Studies demonstrated that Escherichia coli (E. coli) efflux cysteine to the periplasm by CydDC transporters to regulate the redoxs status of the periplasm. 15) The disturbance of the redoxs status in the periplasm in CydDC mutants supported this view. It has also been shown that plasma thiol levels are implicated in cardiovascular diseases.…”

Section: Introductionmentioning

confidence: 86%

Hyperosmolarity Induced Cystine Transport and Cystine-cysteine Cycle between Erythrocytes and the Plasma

Yıldız

Cakir

2008

JOURNAL OF HEALTH SCIENCE

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The objective of the present study was to determine if a cystine-cysteine cycle operates between the erythrocytes and the plasma. In the present study we incubated the erythrocytes in krebs ringer phosphate buffer with different osmolarity containing different amounts of cystine. Our results show that erythrocytes do not uptake cystine from the environment when the osmolarity of the buffer is 310 mOsmol/l. Erythrocytes also do not operate a cystinecysteine cycle in this isoosmolar buffer. However, when exposed to hyperosmolar buffer in the ranges that occur in the kidney medulla which is in between 1200-1400 mOsmol/l erythrocytes start to uptake cystine from the environment and induce a cystine-cysteine cycle. The cystine uptake and cystine-cysteine cycle were characterized by measurement of changes in the free -SH concentrations in erythrocytes and in the buffer. Following incubation of erythrocytes in 1 mM cystine containing 1250 and 1300 mOsmol/l buffer, the free -SH concentrations in the buffer reached to 0.102 ± 0.002 and 0.241 ± 0.013 µmol/ml erythrocyte respectively. Our results demonstrate that erythrocytes display a cystine-cysteine cycle in hyperosmolar environment which is prevailed mainly in the kidney medulla. Our results also display that this process is biologically active and energy dependent. The observed cystine-cysteine cycle is inhibited when the erythrocytes are incubated at lower temperatures and in the absence of glucose. Our results suggest that erythrocytes uptake cystine, intracellulary reduce it to cysteine and release it back to the environment when exposed to hyperosmolar conditions. Erythrocytes may have a role in the regulation of plasma cystine and cysteine concentrations and may contribute to the regulation of plasma redox status.

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Cysteine Is Exported from the Escherichia coliCytoplasm by CydDC, an ATP-binding Cassette-type Transporter Required for Cytochrome Assembly

Cited by 107 publications

References 65 publications

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

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

Role of Cytochrome bd Oxidase from Corynebacterium glutamicum in Growth and Lysine Production

Hyperosmolarity Induced Cystine Transport and Cystine-cysteine Cycle between Erythrocytes and the Plasma

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