Different subcellular locations of secretome components of Gram-positive bacteria

Buist, Girbe; Ridder, Anja N. J. A.; Kok, Jan; Kuipers, Oscar P.

doi:10.1099/mic.0.29113-0

Cited by 38 publications

(32 citation statements)

References 56 publications

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“…Assays of PhoA activity on indicator plates and in liquid culture confirmed that YneA is exported, and based on plate growth and morphology, YneA-PhoA is partially functional (data not shown). Since proteins translocated across the membrane may remain linked to the membrane, associate with the cell wall, or be released into the surrounding medium (12,53), we wanted to determine where the YneA protein localized. We separated cells expressing yneA-phoA into cell-associated, wall-associated, and secreted fractions.…”

Section: Resultsmentioning

confidence: 99%

YneA, an SOS-Induced Inhibitor of Cell Division in Bacillus subtilis , Is Regulated Posttranslationally and Requires the Transmembrane Region for Activity

Burkholder

2010

J Bacteriol

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Cell viability depends on the stable transmission of genetic information to each successive generation. Therefore, in the event of intrinsic or extrinsic DNA damage, it is important that cell division be delayed until DNA repair has been completed. In Bacillus subtilis, this is accomplished in part by YneA, an inhibitor of division that is induced as part of the SOS response. We sought to gain insight into the mechanism by which YneA blocks cell division and the processes involved in shutting off YneA activity. Our data suggest that YneA is able to inhibit daughter cell separation as well as septum formation. YneA contains a LysM peptidoglycan binding domain and is predicted to be exported. We established that the YneA signal peptide is rapidly cleaved, resulting in secretion of YneA into the medium. Mutations within YneA affect both the rate of signal sequence cleavage and the activity of YneA. YneA does not stably associate with the cell wall and is rapidly degraded by extracellular proteases. Based on these results, we hypothesize that exported YneA is active prior to signal peptide cleavage and that proteolysis contributes to the inactivation of YneA. Finally, we identified mutations in the transmembrane segment of YneA that abolish the ability of YneA to inhibit cell division, while having little or no effect on YneA export or stability. These data suggest that protein-protein interactions mediated by the transmembrane region may be required for YneA activity.

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Section: Resultsmentioning

confidence: 99%

YneA, an SOS-Induced Inhibitor of Cell Division in Bacillus subtilis , Is Regulated Posttranslationally and Requires the Transmembrane Region for Activity

Burkholder

2010

J Bacteriol

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“…In Gram-positive bacteria, proteins can be sorted to four different destinations: the cytoplasm, the membrane, the cell wall and the extracellular environment (Buist et al, 2006). The study of the cytoplasmic proteome of B. longum under different gastrointestinal conditions (pH and bile) in vitro (Sánchez et al, 2005(Sánchez et al, , 2007 and in vivo (Yuan et al, 2008) was accomplished in previous studies.…”

Section: Discussionmentioning

confidence: 99%

The cell-envelope proteome of Bifidobacterium longum in an in vitro bile environment

et al. 2009

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Host-bacteria interactions are often mediated via surface-associated proteins. The identification of these proteins is an important goal of bacterial proteomics. To address how bile can influence the cell-envelope proteome of Bifidobacterium longum biotype longum NCIMB 8809, we analysed its membrane protein fraction using stable isotope labelling of amino acids in cell culture (SILAC). We were able to identify 141 proteins in the membrane fraction, including a large percentage of the theoretical transporters of this species. Moreover, the envelope-associated soluble fraction was analysed using different subfractionation techniques and differential in-gel fluorescence electrophoresis (DIGE). This approach identified 128 different proteins. Some of them were well-known cell wall proteins, but others were highly conserved cytoplasmic proteins probably displaying a 'moonlighting' function. We were able to identify 11 proteins in the membrane fraction and 6 proteins in the envelope-associated soluble fraction whose concentration varied in the presence of bile. Bile promoted changes in the levels of proteins with important biological functions, such as some ribosomal proteins and enolase. Also, oligopeptide-binding proteins were accumulated on the cell surface, which was reflected in a different tripeptide transport rate in the cells grown with bile. The data reported here will provide the first cell-envelope proteome map for B. longum, and may contribute to understanding the bile tolerance of these bacteria

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“…The issue of surface-associated proteins, among other protein groups supporting probiotic action in probiotic bacteria, has recently been extensively reviewed by Lebeer and co-workers (Lebeer et al, 2008(Lebeer et al, , 2010, by Kleerebezem et al (2010) and by Buist et al (2006). Another recent report has focused on the adhesins present in one of the major probiotic groups, the genus Lactobacillus (Vélez et al, 2007).…”

Section: Proteins Secreted By Probiotic Bacteriamentioning

confidence: 99%

Extracellular proteins secreted by probiotic bacteria as mediators of effects that promote mucosa–bacteria interactions

2010

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During the last few years, a substantial body of scientific evidence has accumulated suggesting that certain surface-associated and extracellular components produced by probiotic bacteria could be responsible for some of their mechanisms of action. These bacterial components would be able to directly interact with the host mucosal cells; they include exopolysaccharides, bacteriocins, lipoteichoic acids and surface-associated and extracellular proteins. Extracellular proteins include proteins that are actively transported to the bacterial surroundings through the cytoplasmic membrane, as well as those that are simply shed from the bacterial surface. Compared to the other bacterial components, the interactive ability of extracellular proteins/ peptides has been less extensively studied. In this review, current findings supporting an interaction between extracellular proteins/peptides produced by probiotic bacteria (strains of the genera Bifidobacterium, Lactobacillus and Escherichia) and host mucosal cells are discussed. Research needs and future trends are also considered.

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Different subcellular locations of secretome components of Gram-positive bacteria

Cited by 38 publications

References 56 publications

YneA, an SOS-Induced Inhibitor of Cell Division in Bacillus subtilis , Is Regulated Posttranslationally and Requires the Transmembrane Region for Activity

YneA, an SOS-Induced Inhibitor of Cell Division in Bacillus subtilis , Is Regulated Posttranslationally and Requires the Transmembrane Region for Activity

The cell-envelope proteome of Bifidobacterium longum in an in vitro bile environment

Extracellular proteins secreted by probiotic bacteria as mediators of effects that promote mucosa–bacteria interactions

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