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

Pittman, Marc S.; Robinson, H. C.; Poole, Robert K.

doi:10.1074/jbc.m503075200

Cited by 165 publications

(149 citation statements)

References 71 publications

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“…5A). CydDC proteins are responsible for transport of glutathione from the cytoplasm to the periplasmic space for maintenance of the optimum redox balance in this compartment (52,53), and therefore, it would make biological sense to down-regulate these transporters when the environment becomes depleted for oxygen.…”

Section: Discussionmentioning

confidence: 99%

“…This operon encodes an ATP-dependent transporter of glutathione required for maintaining balanced redox control in the periplasm and for assembling cytochrome c and periplasmic cytochrome bd (52,53). Furthermore, the yceJI operon encodes a cytochrome b561 homolog that was reported to be negatively regulated by FNR (32)(33)(34).…”

Section: Srna-regulated Anaerobic Gene Expression In E Colimentioning

confidence: 99%

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Translational Regulation of Gene Expression by an Anaerobically Induced Small Non-coding RNA in Escherichia coli

Boysen

Møller‐Jensen

Kallipolitis

et al. 2010

Journal of Biological Chemistry

101

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Small non-coding RNAs (sRNA) have emerged as important elements of gene regulatory circuits. In enterobacteria such as Escherichia coli and Salmonella many of these sRNAs interact with the Hfq protein, an RNA chaperone similar to mammalian Sm-like proteins and act in the post-transcriptional regulation of many genes. A number of these highly conserved ribo-regulators are stringently regulated at the level of transcription and are part of major regulons that deal with the immediate response to various stress conditions, indicating that every major transcription factor may control the expression of at least one sRNA regulator. Here, we extend this view by the identification and characterization of a highly conserved, anaerobically induced small sRNA in E. coli, whose expression is strictly dependent on the anaerobic transcriptional fumarate and nitrate reductase regulator (FNR). The sRNA, named FnrS, possesses signatures of base-pairing RNAs, and we show by employing global proteomic and transcriptomic profiling that the expression of multiple genes is negatively regulated by the sRNA. Intriguingly, many of these genes encode enzymes with "aerobic" functions or enzymes linked to oxidative stress. Furthermore, in previous work most of the potential target genes have been shown to be repressed by FNR through an undetermined mechanism. Collectively, our results provide insight into the mechanism by which FNR negatively regulates genes such as sodA, sodB, cydDC, and metE, thereby demonstrating that adaptation to anaerobic growth involves the action of a small regulatory RNA.In recent years non-coding RNAs have emerged as important components of regulatory circuits both in bacteria and eukaryotes (1-3). In enteric bacteria such as Escherichia coli and Salmonella more than a hundred different sRNAs 2 have been identified, and a major class consists of trans-encoded gene regulatory RNAs that act by an antisense mechanism to activate or, more frequently, to repress translation of target mRNAs. Many of these sRNAs are conserved in related species, are made in response to changes in environmental conditions, and are required for adaptation to stress or specific growth conditions. Several common features have been uncovered. First, the sRNA genes are generally highly regulated at the transcriptional level and are frequently expressed as components of global regulatory systems. Well studied regulatory cases include OxyR regulation of OxyS RNA (oxidative stress) (4), Fur regulation of RyhB RNA (iron limitation) (5), cAMP-CRP regulation of CyaR and Spot 42 RNA (glucose limitation) (6 -9), OmpR regulation of MicF, OmrA, and OmrB RNAs (osmotic shock) (10, 11), E -mediated transcription of MicA and RybB RNAs (envelope stress) (2, 12), PhoPQ regulation of MgrR (Mg 2ϩ /Ca 2ϩ transport and virulence) (13), and LuxO control of Qrr1-4 (quorum sensing in Vibrio) (14). Furthermore, small RNA expression may be under control of a dedicated transcription factor, as exemplified by SgrR/SgrS RNA (glucose-phosphate stress) (15). Second, pairin...

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Section: Discussionmentioning

confidence: 99%

Section: Srna-regulated Anaerobic Gene Expression In E Colimentioning

confidence: 99%

Translational Regulation of Gene Expression by an Anaerobically Induced Small Non-coding RNA in Escherichia coli

Boysen

Møller‐Jensen

Kallipolitis

et al. 2010

Journal of Biological Chemistry

101

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“…GrxC Pdependent motility was enhanced on rich media compared to minimal media (Table 1) perhaps due to the presence of small oxidizing molecules, such as glutathione, present in rich media (1). In minimal media, there may be sufficient export of glutathione from the cytoplasm (13,14) to allow the oxidation reaction to occur in minimal medium. If the oxidative activity of GrxC P is dependent on oxidized glutathione, then mutations that eliminate glutathione biosynthesis should prevent the oxidation of substrates from taking place.…”

Section: Oxidative Activity Of Grxcp Depends On the Cytoplasmic Glutamentioning

confidence: 99%

“…We have also examined the effects of mutations in several genes, including cydD (encoding a proposed glutathione exporter), ggt (encoding periplasmic ␥-glutamyl transpeptidase), and mdlA (encoding a multidrug resistant-like ABC transporter) (13,30,31), which might influence the concentration of periplasmic glutathione. However, none of these mutations affected the ability of GrxC P to promote disulfide bond formation in AP (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm

Eser

Masip

Kadokura

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Organisms have evolved elaborate systems that ensure the homeostasis of the thiol redox environment in their intracellular compartments. In Escherichia coli, the cytoplasm is kept under reducing conditions by the thioredoxins with the help of thioredoxin reductase and the glutaredoxins with the small molecule glutathione and glutathione reductase. As a result, disulfide bonds are constantly resolved in this compartment. In contrast to the cytoplasm, the periplasm of E. coli is maintained in an oxidized state by DsbA, which is recycled by DsbB. Thioredoxin 1, when exported to the periplasm turns from a disulfide bond reductase to an oxidase that, like DsbA, is dependent on DsbB. In this study we set out to investigate whether a subclass of the thioredoxin superfamily, the glutaredoxins, can become disulfide bond-formation catalysts when they are exported to the periplasm. We find that glutaredoxins can promote disulfide bond formation in the periplasm. However, contrary to the behavior of thioredoxin 1 in this environment, the glutaredoxins do so independently of DsbB. Furthermore, we show that glutaredoxin 3 requires the glutathione biosynthesis pathway for its function and can oxidize substrates with only a single active-site cysteine. Our data provides in vivo evidence suggesting that oxidized glutathione is present in the E. coli periplasm in biologically significant concentrations.protein oxidation ͉ monothiol ͉ SRP

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

Cited by 165 publications

References 71 publications

Translational Regulation of Gene Expression by an Anaerobically Induced Small Non-coding RNA in Escherichia coli

Translational Regulation of Gene Expression by an Anaerobically Induced Small Non-coding RNA in Escherichia coli

Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm

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

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