Identification of the arginine/ornithine antiporter ArcD from <i>Halobacterium salinarum</i>

Wimmer, Florian; Oberwinkler, Tanja; Bisle, Birgit; Tittor, Jörg; Oesterhelt, Dieter

doi:10.1016/j.febslet.2008.10.004

Cited by 20 publications

(18 citation statements)

References 18 publications

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“…Similar to ArcD of Lactococcus ( Streptococcus ) lactis , ArcD facilitates an ATP-independent, electro-neutral exchange of arginine and ornithine across the bacterial membrane, thereby providing a substrate for ADS mediated arginine catabolism (Driessen et al, 1987; Verhoogt et al, 1992; Bourdineaud et al, 1993). The putative function of ArcD as an arginine-ornithine antiporter was also shown by Wimmer et al for the archaeon Halobacterium salinarum (Wimmer et al, 2008). On the other hand, an involvement of ArcD in virulence is yet speculative.…”

Section: Introductionsupporting

confidence: 56%

The arginine-ornithine antiporter ArcD contributes to biological fitness of Streptococcus suis

Fulde¹,

Willenborg²,

Huber³

et al. 2014

Front. Cell. Infect. Microbiol.

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The arginine-ornithine antiporter (ArcD) is part of the Arginine Deiminase System (ADS), a catabolic, energy-providing pathway found in a variety of different bacterial species, including the porcine zoonotic pathogen Streptococcus suis. The ADS has recently been shown to play a role in the pathogenicity of S. suis, in particular in its survival in host cells. The contribution of arginine and arginine transport mediated by ArcD, however, has yet to be clarified. In the present study, we showed by experiments using [U-13C6]arginine as a tracer molecule that S. suis is auxotrophic for arginine and that bacterial growth depends on the uptake of extracellular arginine. To further study the role of ArcD in arginine metabolism, we generated an arcD-specific mutant strain and characterized its growth compared to the wild-type (WT) strain, a virulent serotype 2 strain. The mutant strain showed a markedly reduced growth in chemically defined media supplemented with arginine when compared to the WT strain, suggesting that ArcD promotes arginine uptake. To further evaluate the in vivo relevance of ArcD, we studied the intracellular bacterial survival of the arcD mutant strain in an epithelial cell culture infection model. The mutant strain was substantially attenuated, and its reduced intracellular survival rate correlated with a lower ability to neutralize the acidified environment. Based on these results, we propose that ArcD, by its function as an arginine-ornithine antiporter, is important for supplying arginine as substrate of the ADS and, thereby, contributes to biological fitness and virulence of S. suis in the host.

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Section: Introductionsupporting

confidence: 56%

The arginine-ornithine antiporter ArcD contributes to biological fitness of Streptococcus suis

Fulde¹,

Willenborg²,

Huber³

et al. 2014

Front. Cell. Infect. Microbiol.

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“…NRC-1 is a part of the arcRACB operon that encodes enzymes for fermentative growth via the arginine deiminase pathway [138]. An arginine-ornithine antiporter gene, arcD , is located immediately downstream of this operon and is also the part of this pathway [139]. A putative ArcR ortholog in Hfx.…”

Section: Resultsmentioning

confidence: 99%

The Complete Genome Sequence of Haloferax volcanii DS2, a Model Archaeon

et al. 2010

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Background Haloferax volcanii is an easily culturable moderate halophile that grows on simple defined media, is readily transformable, and has a relatively stable genome. This, in combination with its biochemical and genetic tractability, has made Hfx. volcanii a key model organism, not only for the study of halophilicity, but also for archaeal biology in general.Methodology/Principal FindingsWe report here the sequencing and analysis of the genome of Hfx. volcanii DS2, the type strain of this species. The genome contains a main 2.848 Mb chromosome, three smaller chromosomes pHV1, 3, 4 (85, 438, 636 kb, respectively) and the pHV2 plasmid (6.4 kb).Conclusions/SignificanceThe completed genome sequence, presented here, provides an invaluable tool for further in vivo and in vitro studies of Hfx. volcanii.

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“…In Natronobacterium gregoryi SP1, another archaeon, a homolog of the transporter is found 4 kb downstream of the arcABC cluster. The transporter of Halobacterium salinarum was demonstrated to be the L‐arginine/L‐ornithine exchanger in the ADI pathway (Wimmer, Oberwinkler, Bisle, Tittor, & Oesterhelt, ). The NhaC transporter shows no significant sequence identity with the ArcD and ArcE proteins and may provide another example of a transporter that functionally converged to L‐arginine/L‐ornithine exchange activity.…”

Section: Discussionmentioning

confidence: 99%

Convergent evolution of the arginine deiminase pathway: the ArcD and ArcE arginine/ornithine exchangers

Noens

Lolkema

2016

MicrobiologyOpen

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The arginine deiminase (ADI) pathway converts L‐arginine into L‐ornithine and yields 1 mol of ATP per mol of L‐arginine consumed. The L‐arginine/L‐ornithine exchanger in the pathway takes up L‐arginine and excretes L‐ornithine from the cytoplasm. Analysis of the genomes of 1281 bacterial species revealed the presence of 124 arc gene clusters encoding the pathway. About half of the clusters contained the gene encoding the well‐studied L‐arginine/L‐ornithine exchanger ArcD, while the other half contained a gene, termed here arcE, encoding a membrane protein that is not a homolog of ArcD. The arcE gene product of Streptococcus pneumoniae was shown to take up L‐arginine and L‐ornithine with affinities of 0.6 and 1 μmol/L, respectively, and to catalyze metabolic energy‐independent, electroneutral exchange. ArcE of S. pneumoniae could replace ArcD in the ADI pathway of Lactococcus lactis and provided the cells with a growth advantage. In contrast to ArcD, ArcE catalyzed translocation of the pathway intermediate L‐citrulline with high efficiency. A short version of the ADI pathway is proposed for L‐citrulline catabolism and the presence of the evolutionary unrelated arcD and arcE genes in different organisms is discussed in the context of the evolution of the ADI pathway.

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Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum

Cited by 20 publications

References 18 publications

The arginine-ornithine antiporter ArcD contributes to biological fitness of Streptococcus suis

The arginine-ornithine antiporter ArcD contributes to biological fitness of Streptococcus suis

The Complete Genome Sequence of Haloferax volcanii DS2, a Model Archaeon

Convergent evolution of the arginine deiminase pathway: the ArcD and ArcE arginine/ornithine exchangers

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