Repair of Oxidized Proteins

Grimaud, Régis; Ezraty, Benjamin; Mitchell, Jennifer K; Lafitte, Daniel; Briand, Claudette; Derrick, Peter J.; Barras, Frédéric

doi:10.1074/jbc.m105509200

Cited by 321 publications

(115 citation statements)

References 35 publications

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“…Fragments of Lsp were probably eluted from the gel together with the 185-kDA Methionine-sulfoxide reductase (Msr) reverses the loss of biological activity of proteins caused by oxidation of methionine to methionine sulfoxide (2). Most bacteria contain at least two genes encoding Msr activity, namely, msrA (msrA1, msrA2, and msrA3 in the case of Staphylococcus aureus) and msrB (11,26). MsrA and msrB show substrate specificity for the two diastereomeric forms of methionine sulfoxide (MetO): R-MetO and S-MetO (17,26).…”

Section: Discussionmentioning

confidence: 99%

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A High-Molecular-Mass Surface Protein (Lsp) and Methionine Sulfoxide Reductase B (MsrB) Contribute to the Ecological Performance of Lactobacillus reuteri in the Murine Gut

Walter

Chagnaud

Tannock

et al. 2005

Appl Environ Microbiol

114

125

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Members of the genus Lactobacillus are common inhabitants of the gut, yet little is known about the traits that contribute to their ecological performance in gastrointestinal ecosystems. Lactobacillus reuteri 100-23 persists in the gut of the reconstituted Lactobacillus-free mouse after a single oral inoculation. Recently, three genes of this strain that were specifically induced (in vivo induced) in the murine gut were identified (38). We report here the detection of a gene of L. reuteri 100-23 that encodes a high-molecular-mass surface protein (Lsp) that shows homology to proteins involved in the adherence of other bacteria to epithelial cells and in biofilm formation. The three in vivo-induced genes and lsp of L. reuteri 100-23 were inactivated by insertional mutagenesis in order to study their biological importance in the murine gastrointestinal tract. Competition experiments showed that mutation of lsp and a gene encoding methionine sulfoxide reductase (MsrB) reduced ecological performance. Mutation of lsp impaired the adherence of the bacteria to the epithelium of the mouse forestomach and altered colonization dynamics. Homologues of lsp and msrB are present in the genomes of several strains of Lactobacillus and may play an important role in the maintenance of these bacteria in gut ecosystems.The guts of mammals are colonized by a complex collection of microorganisms (the gut microbiota) that influence biochemical, physiological, immunological, and nonspecific disease resistance characteristics of the host (10). The bacterial composition of this ecosystem has been shown to be remarkably stable over time (43). Members of the gut microbiota have presumably coevolved with their host species and must possess traits that enable them to establish and maintain themselves in a lotic (flowing) and competitive environment. On the other hand, there are microbes present in the gastrointestinal tract that have a transient existence (allochthonous components), and this situation raises questions about what factors distinguish resident members of the microbiota from allochthonous members (27).Lactobacillus reuteri strain 100-23 is a true (autochthonous) resident of the murine gut because it adheres to the nonsecretory epithelium of the forestomach and persists at constant population levels in particular regions of the gut throughout the life of the murine host (13, 39).We maintain a colony of mice whose gut microbiota is devoid of lactobacilli but is otherwise equivalent to that of conventional mice (32). These reconstituted Lactobacillus-free (RLF) mice permit the study of Lactobacillus traits against a standardized bacteriological background. L. reuteri 100-23 and the RLF mouse gut therefore provide an appropriate model system with which to study the molecular basis of Lactobacillus autochthony.While L. reuteri 100-23 inhabits the murine gut, genes encoding methionine sulfoxide reductase (msrB), xylose isomerase (xylA), and a protein with low similarity to methionine synthase II (met) are specifically induced (38). Add...

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Section: Discussionmentioning

confidence: 99%

“…MsrA and msrB show substrate specificity for the two diastereomeric forms of methionine sulfoxide (MetO): R-MetO and S-MetO (17,26). Homologues to msrA and msrB are present in the genomes of virtually all bacteria (2,11), including Lactobacillus spp. (L. johnsonii, L. gasseri, and Lactobacillus plantarum).…”

Section: Discussionmentioning

confidence: 99%

A High-Molecular-Mass Surface Protein (Lsp) and Methionine Sulfoxide Reductase B (MsrB) Contribute to the Ecological Performance of Lactobacillus reuteri in the Murine Gut

Walter

Chagnaud

Tannock

et al. 2005

Appl Environ Microbiol

114

125

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“…Two types of this enzyme (MsrA and MsrB) have been described, and all organisms that have been studied contain MsrA (3). Almost all free-living organisms except a few archaebacteria contain MsrB (6). Despite being functionally related, MsrA and MsrB failed to exhibit any overall sequence similarity (6).…”

Section: Discussionmentioning

confidence: 99%

Identification of Lactobacillus reuteri Genes Specifically Induced in the Mouse Gastrointestinal Tract

Walter

Heng

Hammes

et al. 2003

Appl Environ Microbiol

114

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Lactobacilli are common inhabitants of the gastrointestinal tracts of mammals and have received considerable attention due to their putative health-promoting properties. Little is known about the traits that enhance the ability of these bacteria to inhabit the gastrointestinal tract. In this paper we describe the development and application of a strategy based on in vivo expression technology (IVET) that enables detection of Lactobacillus reuteri genes specifically induced in the murine gut. A plasmid-based system was constructed containing ermGT (which confers lincomycin resistance) as the primary reporter gene for selection of promoters active in the gastrointestinal tract of mice treated with lincomycin. A second reporter gene, bglM (␤-glucanase), allowed differentiation between constitutive and in vivo inducible promoters. The system was successfully tested in vitro and in vivo by using a constitutive promoter. Application of the IVET system with chromosomal DNA of L. reuteri 100-23 and reconstituted lactobacillus-free mice revealed three genes induced specifically during colonization. Two of the sequences showed homology to genes encoding xylose isomerase (xylA) and peptide methionine sulfoxide reductase (msrB), which are involved in nutrient acquisition and stress responses, respectively. The third locus showed homology to the gene encoding a protein whose function is not known. Our IVET system has the potential to identify genes of lactobacilli that have not previously been functionally characterized but which may be essential for growth of these bacteria in the gastrointestinal ecosystem.The gastrointestinal tracts of vertebrate animals are colonized by a complex microflora containing several hundred different species, some of which are present at high levels (29). Bacteria belonging to the genus Lactobacillus are common inhabitants of this ecosystem and have received considerable attention due to their putative health-promoting properties when they are ingested as probiotics (19,36). Lactobacillus species comprise only a minor part of the bacterial community in human feces (19,25), but in animals such as pigs, chickens, mice, and rats lactobacilli are the predominant bacteria in proximal regions of the gut. They can also be detected as minority members of the large bowel ecosystem in these animals (19). In order to persist in the gastrointestinal tract, which is a lotic and highly competitive ecosystem, the bacteria must have appropriate multiplication rates and metabolic activities. Ecological studies have suggested that only a minority of the lactobacilli found in intestinal samples meet these requirements and are truly autochthonous, but the bacterial factors that allow lactobacilli to become established and persist in the gastrointestinal tract are unknown (22,34,37).In the last decade, promoter-trapping technologies have been developed to overcome the limitations of in vitro models for studying the traits that enhance ecological performance in complex ecosystems. In vivo expression technology (IVET...

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“…Crude extracts show little MsrB activity, and the recombinant enzyme has significantly lower activity for free Met-(R)-O when compared with the MsrA enzymes (5). Thus, it is unclear how MsrB could enable an E. coli Met auxotroph to grow on Met-(R)-O as a Met source (6).…”

mentioning

confidence: 99%

Free methionine-( R )-sulfoxide reductase from Escherichia coli reveals a new GAF domain function

Zhi-dong

Johnson

Weissbach

et al. 2007

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

126

138

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The reduction of methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr). The MsrA and MsrB families can reduce free MetO and MetO within a peptide or protein context. This process is stereospecific with the S-and R-forms of MetO repaired by MsrA and MsrB, respectively. Cell extracts from an MsrA ؊ B ؊ knockout of Escherichia coli have several remaining Msr activities. This study has identified an enzyme specific for the free form of Met-(R)-O, fRMsr, through proteomic analysis. The recombinant enzyme exhibits the same substrate specificity and is as active as MsrA family members. E. coli fRMsr is, however, 100-to 1,000-fold more active than non-selenocysteine-containing MsrB enzymes for free Met-(R)-O. The crystal structure of E. coli fRMsr was previously determined, but no known function was assigned. Thus, the function of this protein has now been determined. The structural similarity of the E. coli and yeast proteins suggests that most fRMsrs use three cysteine residues for catalysis and the formation of a disulfide bond to enclose a small active site cavity. This latter feature is most likely a key determinant of substrate specificity. Moreover, E. coli fRMsr is the first GAF domain family member to show enzymatic activity. Other GAF domain proteins substitute the Cys residues and others to specifically bind cyclic nucleotides, chromophores, and many other ligands for signal potentiation. Therefore, Met-(R)-O may represent a signaling molecule in response to oxidative stress and nutrients via the TOR pathway in some organisms. methionine oxidation ͉ methionine sulfoxide reductase

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Repair of Oxidized Proteins

Cited by 321 publications

References 35 publications

A High-Molecular-Mass Surface Protein (Lsp) and Methionine Sulfoxide Reductase B (MsrB) Contribute to the Ecological Performance of Lactobacillus reuteri in the Murine Gut

A High-Molecular-Mass Surface Protein (Lsp) and Methionine Sulfoxide Reductase B (MsrB) Contribute to the Ecological Performance of Lactobacillus reuteri in the Murine Gut

Identification of Lactobacillus reuteri Genes Specifically Induced in the Mouse Gastrointestinal Tract

Free methionine-( R )-sulfoxide reductase from Escherichia coli reveals a new GAF domain function

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