Methionine Sulfoxide Reduction and Assimilation in
            <i>Escherichia coli</i>
            : New Role for the Biotin Sulfoxide Reductase BisC

Ezraty, Benjamin; Bos, Julia; Barras, Frédéric; Aussel, Laurent

doi:10.1128/jb.187.1.231-237.2005

Cited by 60 publications

(65 citation statements)

References 32 publications

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“…In E. coli, the bisC-encoded biotin sulfoxide reductase is able to reduce both biotin sulfoxide and methionine sulfoxide to biotin and methionine, respectively (41). This dual activity for BisC also was recently demonstrated in Salmonella enterica serovar Typhimurium and linked to the survival of this organism under conditions of oxidative stress.…”

Section: Discussionmentioning

confidence: 95%

bis -Molybdopterin Guanine Dinucleotide Is Required for Persistence of Mycobacterium tuberculosis in Guinea Pigs

et al. 2015

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e Mycobacterium tuberculosis is able to synthesize molybdopterin cofactor (MoCo), which is utilized by numerous enzymes that catalyze redox reactions in carbon, nitrogen, and sulfur metabolism. In bacteria, MoCo is further modified through the activity of a guanylyltransferase, MobA, which converts MoCo to bis-molybdopterin guanine dinucleotide (bis-MGD), a form of the cofactor that is required by the dimethylsulfoxide (DMSO) reductase family of enzymes, which includes the nitrate reductase NarGHI. In this study, the functionality of the mobA homolog in M. tuberculosis was confirmed by demonstrating the loss of assimilatory and respiratory nitrate reductase activity in a mobA deletion mutant. This mutant displayed no survival defects in human monocytes or mouse lungs but failed to persist in the lungs of guinea pigs. These results implicate one or more bis-MGDdependent enzymes in the persistence of M. tuberculosis in guinea pig lungs and underscore the applicability of this animal model for assessing the role of molybdoenzymes in this pathogen.

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Section: Discussionmentioning

confidence: 95%

bis -Molybdopterin Guanine Dinucleotide Is Required for Persistence of Mycobacterium tuberculosis in Guinea Pigs

et al. 2015

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“…Biotine sulfoxide reductase BisC (19) was another candidate that could play a role in selenite reduction, since this molybdoenzyme has been shown to exhibit a wide substrate specificity in vitro, including biotin sulfoxide, DMSO, trimethylamine oxide, and methionine-S-sulfoxide (5,18). In addition, the corresponding gene, bisC, was not present in Rhodobacter sphaeroides 2.4.1, a strain exhibiting a very low level of selenite reduction activity (10-fold lower than R. sphaeroides f. sp.…”

Section: Resultsmentioning

confidence: 99%

Genetic and Biochemical Evidence for the Involvement of a Molybdenum-Dependent Enzyme in One of the Selenite Reduction Pathways ofRhodobacter sphaeroidesf. sp.denitrificansIL106

Pierru

Grosse

Pignol

et al. 2006

Appl Environ Microbiol

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Selenite reduction in Rhodobacter sphaeroides f. sp. denitrificans was observed under photosynthetic conditions, following a 100-h lag period. This adaptation period was suppressed if the medium was inoculated with a culture previously grown in the presence of selenite, suggesting that selenite reduction involves an inducible enzymatic pathway. A transposon library was screened to isolate mutants affected in selenite reduction. Of the eight mutants isolated, two were affected in molybdenum cofactor synthesis. These moaA and mogA mutants showed an increased duration of the lag phase and a decreased rate of selenite reduction. When grown in the presence of tungstate, a well-known molybdenum-dependent enzyme (molybdoenzyme) inhibitor, the wild-type strain displayed the same phenotype. The addition of tungstate in the medium or the inactivation of the molybdocofactor synthesis induced a decrease of 40% in the rate of selenite reduction. These results suggest that several pathways are involved and that one of them involves a molybdoenzyme. Although addition of nitrate or dimethyl sulfoxide (DMSO) to the medium increased the selenite reduction activity of the culture, neither the periplasmic nitrate reductase NAP nor the DMSO reductase is the implicated molybdoenzyme, since the napA and dmsA mutants, with expression of nitrate reductase and DMSO reductase, respectively, eliminated, were not affected by selenite reduction. A role for the biotine sulfoxide reductase, another characterized molybdoenzyme, is unlikely, since its overexpression in a defective strain did not restore the selenite reduction activity.

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“…E. coli produces a non-exported biotin sulfoxide/methionine sulfoxide reductase encoded by the bisC gene (Ezraty et al, 2005;Pierson & Campbell, 1990). BisC is a homologue of the well-characterized E. coli Tat substrate trimethylamine N-oxide (TMAO) reductase (TorA) (Mejean et al, 1994), but is a cytoplasmic enzyme with an N-tail analogous to that identified on NarG (Ezraty et al, 2005;Sargent, 2007b;Turner et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains

et al. 2009

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The twin-arginine translocation (Tat) pathway is a prokaryotic protein targeting system dedicated to the transmembrane translocation of folded proteins. Substrate proteins are directed to the Tat translocase by signal peptides bearing a conserved SRRxFLK ‘twin-arginine’ motif. In Escherichia coli, most of the 27 periplasmically located Tat substrates are cofactor-containing respiratory enzymes, and many of these harbour a molybdenum cofactor at their active site. Molybdenum cofactor-containing proteins are not exclusively located in the periplasm, however, with the major respiratory nitrate reductase (NarG) and the biotin sulfoxide reductase (BisC), for example, being located at the cytoplasmic side of the membrane. Interestingly, both NarG and BisC contain ‘N-tail’ regions that bear some sequence similarity to twin-arginine signal peptides. In this work, we have examined the relationship between the non-exported N-tails and the Tat system. Using a sensitive genetic screen for Tat transport, variant N-tails were identified that displayed Tat transport activity. For the NarG 36-residue N-tail, six amino acid changes were needed to induce transport activity. However, these changes interfered with binding by the NarJ biosynthetic chaperone and impaired biosynthesis of the native enzyme. For the BisC 36-residue N-tail, only five amino acid substitutions were needed to restore Tat transport activity. These modifications also impaired in vivo BisC activity, but it was not possible to identify a biosynthetic chaperone for this enzyme. These data highlight an intimate genetic and evolutionary link between some non-exported redox enzymes and those transported across membranes by the Tat translocation system.

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Methionine Sulfoxide Reduction and Assimilation in Escherichia coli : New Role for the Biotin Sulfoxide Reductase BisC

Cited by 60 publications

References 32 publications

bis -Molybdopterin Guanine Dinucleotide Is Required for Persistence of Mycobacterium tuberculosis in Guinea Pigs

bis -Molybdopterin Guanine Dinucleotide Is Required for Persistence of Mycobacterium tuberculosis in Guinea Pigs

Genetic and Biochemical Evidence for the Involvement of a Molybdenum-Dependent Enzyme in One of the Selenite Reduction Pathways ofRhodobacter sphaeroidesf. sp.denitrificansIL106

Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains

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