BspA (CyuC) in Lactobacillus fermentum BR11 Is a Highly Expressed High-Affinity L-Cystine-Binding Protein

Hung, Jacky; Turner, Mark S.; Walsh, Tamara; Giffard, Philip M.

doi:10.1007/s00284-004-4408-2

Cited by 23 publications

(22 citation statements)

References 20 publications

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“…This is exactly what we see. The model is consistent with the very high cysteine or cystine concentration requirements for optimal growth of BR11 under aerobic conditions and the evolution of the very high expression level of the CyuC transporter (19). Unlike E. coli, many gram-positive bacteria lack glutathione, but they have other intracellular thiols that perform its function (34).…”

Section: Discussionsupporting

confidence: 63%

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Cystathionine γ-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11

Turner

Barry

et al. 2009

J Bacteriol

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Lactobacillus reuteri BR11 possesses a novel mechanism of oxidative defense involving an abundant cystine ABC transporter encoded by the cyuABC gene cluster. Large amounts of thiols, including H 2 S, are secreted upon cystine uptake by the CyuC transporter. A cystathionine ␥-lyase (cgl) gene is cotranscribed with the cyu genes in several L. reuteri strains and was hypothesized to participate in cystine-mediated oxidative defense by producing reducing equivalents. This hypothesis was tested with L. reuteri BR11 by constructing a cgl mutant (PNG901) and comparing it to a similarly constructed cyuC mutant (PNG902). Although Cgl was required for H 2 S production from cystine, it was not crucial for oxidative defense in de Mann-Rogosa-Sharpe medium, in contrast to CyuC, whose inactivation resulted in lag-phase arrest in aerated cultures. The importance of Cgl in oxidative defense was seen only in the presence of hemin, which poses severe oxidative stress. The growth defects in aerated cultures of both mutants were alleviated by supplementation with cysteine (and cystine in the cgl mutant) but not methionine, with the cyuC mutant showing a much higher concentration requirement. We conclude that L. reuteri BR11 requires a high concentration of exogenous cysteine/cystine to grow optimally under aerobic conditions. This requirement is fulfilled by the abundant CyuC transporter, which has probably arisen due to the broad substrate specificity of Cgl, resulting in a futile pathway which degrades cystine taken up by the CyuC transporter to H 2 S. Cgl plays a secondary role in oxidative defense by its well-documented function of cysteine biosynthesis.

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Section: Discussionsupporting

confidence: 63%

“…1) (45,47). CyuC (formerly BspA) is a highaffinity L-cystine-binding protein that is an abundant component of the cell envelope (19). It is present at approximately 10 5 molecules per cell, which is comparable to the abundance of S-layer subunits.…”

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confidence: 99%

Cystathionine γ-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11

Turner

Barry

et al. 2009

J Bacteriol

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“…Oxidative stress is one of the main factors influencing intestinal injury in IBD [18], with recent studies suggesting that probiotic administration can attenuate oxidative stress in rats [19]. The uptake system of L. reuteri BR11 comprises a high affinity cystine binding protein termed Cystine Uptake C (CyuC), a component of the ATP binding cassette cystine transport system [20]. In order to determine the role of this unique system, the cyuC gene was inactivated using homologous recombination to produce a L. reuteri mutant (PNG201) deficient in cystine uptake [13,21].…”

Section: Lactobacillus Reuteri Br11 (Br11) Is a Bacterial Strain ((Fomentioning

confidence: 99%

Effects of a Lactobacillus reuteri BR11 Mutant Deficient in the Cystine-Transport System in a Rat Model of Inflammatory Bowel Disease

et al. 2011

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“…These systems are rare in prokaryotes, in part because this amino acid is readily oxidized to the disulfide-linked cystine and taken up in this form. For this reason, cystine uptake has been further studied (5,6,17).…”

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A Novel cdsAB Operon Is Involved in the Uptake of l -Cysteine and Participates in the Pathogenesis of Yersinia ruckeri

et al. 2011

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Application of in vivo expression technology (IVET) to Yersinia ruckeri, an important fish pathogen, allowed the identification of two adjacent genes that represent a novel bacterial system involved in the uptake and degradation of L-cysteine. Analysis of the translational products of both genes showed permease domains (open reading frame 1 [ORF1]) and amino acid position identities (ORF2) with the L-cysteine desulfidase from Methanocaldococcus jannaschii, a new type of enzyme involved in the breakdown of L-cysteine. The operon was named cdsAB (cysteine desulfidase) and is found widely in anaerobic and facultative bacteria. cdsAB promoter analysis using lacZY gene fusion showed highest induction in the presence of L-cysteine. Two cdsA and cdsB mutant strains were generated. The limited toxic effect and the low utilization of L-cysteine observed in the cdsA mutant, together with radiolabeled experiments, strongly suggested that CdsA is an L-cysteine permease. Fifty percent lethal dose (LD 50 ) and competence index experiments showed that both the cdsA and cdsB loci were involved in the pathogenesis of the bacteria. In conclusion, this study has shown for the first time in bacteria the existence of an L-cysteine uptake system that together with an additional L-cysteine desulfidase-encoding gene constitutes a novel operon involved in bacterial virulence.

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BspA (CyuC) in Lactobacillus fermentum BR11 Is a Highly Expressed High-Affinity L-Cystine-Binding Protein

Cited by 23 publications

References 20 publications

Cystathionine γ-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11

Cystathionine γ-Lyase Is a Component of Cystine-Mediated Oxidative Defense in Lactobacillus reuteri BR11

Effects of a Lactobacillus reuteri BR11 Mutant Deficient in the Cystine-Transport System in a Rat Model of Inflammatory Bowel Disease

A Novel cdsAB Operon Is Involved in the Uptake of l -Cysteine and Participates in the Pathogenesis of Yersinia ruckeri

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