sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus

Lascelles, June

doi:10.1128/jb.133.2.621-625.1978

Cited by 7 publications

(3 citation statements)

References 14 publications

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“…56 Four enzymes are involved in glycero-phospholipid metabolism (spots 8-10, 82, 83, 96, and 122) such as the glycerol-3phosphate dehydrogenase which is also membrane-associated in S. aureus. 57,58 Three proteins are directly involved in cell wall biogenesis and in peptidoglycan biosynthesis (spots 17, 18, 33, 34, and 95) for example, UDP-N acetylglucosamine transferases. 59 Interestingly, some membrane proteins involved in carbohydrate metabolism could also be involved in cell wall biogenesis such as glucose-6-phosphate isomerase (spots 16 and 17) as shown in Mycobacterium smegmatis, 60 or lactate dehydrogenase (spots 59, 60-76) considering L-lactate could be a cell wall component as observed in Lactobacillus plantarum.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Cell Envelope fromStaphylococcusxylosusC2a, a Coagulase-Negative Staphylococcus

Planchon¹,

Chambon²,

Desvaux³

et al. 2007

J. Proteome Res.

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Staphylococcus xylosus is a saprophytic bacterium commonly found on skin of mammals but also used for its organoleptic properties in manufacturing of fermented meat products. This bacterium is able to form biofilms and to colonize biotic or abiotic surfaces, processes which are mediated, to a certain extent, by cell-envelope proteins. Thus, the present investigation aimed at evaluating and adapting different existing methods for cell-envelope subproteome analyses of the strain S. xylosus C2a. The protocol selected consisted initially of a lysostaphin treatment producing protoplasts and giving a fraction I enriched in cell wall proteins. A second fraction enriched in membrane proteins was then efficiently recovered by a procedure involving delipidation with a mixture of tributyl phosphate, methanol, and acetone and solubilization with a buffer containing ASB14. Proteins were separated using two-dimensional gel electrophoresis (2-DE) and identified using matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS). A total of 168 protein spots was identified corresponding to 90 distinct proteins. To categorize and analyze these proteomic data, a rational bioinformatic approach was carried out on proteins identified within cell envelope of S. xylosus C2a. Thirty-four proteins were predicted as membrane-associated with 91% present, as expected, within fraction II enriched in membrane proteins: 24 proteins were predicted as membranal, 3 as lipoproteins, and 7 as components of membrane protein complex. Eighteen out of 25 (72%) proteins predicted as secreted were indeed identified in fraction I enriched in cell wall proteins: 6 proteins were predicted as secreted via Sec translocon, and the remaining 19 proteins were predicted as secreted via unknown secretion system. Eighty-one percent (25/31) of proteins predicted as cytoplasmic were found in fraction II: 8 were clearly predicted as interacting temporarily with membrane components. By coupling conventional 2-DE and bioinformatic analysis, the approach developed allows fractionating, resolving, and analyzing a significant and important set of cell envelope proteins from a coagulase-negative staphylococcus, that is, S. xylosus C2a.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Cell Envelope fromStaphylococcusxylosusC2a, a Coagulase-Negative Staphylococcus

Planchon¹,

Chambon²,

Desvaux³

et al. 2007

J. Proteome Res.

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“…9A), menaquinone receives electrons directly from a large number of membrane dehydrogenases including glycerol-3-phosphate dehydrogenase, succinate dehydrogenase, the menaquinone oxidase complex, LDH and an NDH2, which in turn receives electrons from at least two solu-ble enzymes: alcohol dehydrogenase and the PDC. In mitochondria LDH and glycerol-3-phosphate dehydrogenase do not donate electrons to the respiratory chain, yet in bacteria they are membrane-bound enzymes transferring their electrons directly to ubiquinol (Barnes and Kaback 1970;Lascelles 1978;Doig et al 1999;Modun and Williams 1999;Dym et al 2000;Delgado et al 2001;Fuller et al 2011). From menaquinone, electrons are transferred to one of two terminal O 2 -dependent oxidases, namely, cytochrome bo and cytochrome aa 3 .…”

Section: Discussionmentioning

confidence: 99%

Staphylococcus epidermidis: metabolic adaptation and biofilm formation in response to different oxygen concentrations

Uribe‐Alvarez

Chiquete-Félix

Contreras-Zentella

et al. 2015

Pathogens and Disease

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Staphylococcus epidermidis has become a major health hazard. It is necessary to study its metabolism and hopefully uncover therapeutic targets. Cultivating S. epidermidis at increasing oxygen concentration [O2] enhanced growth, while inhibiting biofilm formation. Respiratory oxidoreductases were differentially expressed, probably to prevent reactive oxygen species formation. Under aerobiosis, S. epidermidis expressed high oxidoreductase activities, including glycerol-3-phosphate dehydrogenase, pyruvate dehydrogenase, ethanol dehydrogenase and succinate dehydrogenase, as well as cytochromes bo and aa3; while little tendency to form biofilms was observed. Under microaerobiosis, pyruvate dehydrogenase and ethanol dehydrogenase decreased while glycerol-3-phosphate dehydrogenase and succinate dehydrogenase nearly disappeared; cytochrome bo was present; anaerobic nitrate reductase activity was observed; biofilm formation increased slightly. Under anaerobiosis, biofilms grew; low ethanol dehydrogenase, pyruvate dehydrogenase and cytochrome bo were still present; nitrate dehydrogenase was the main terminal electron acceptor. KCN inhibited the aerobic respiratory chain and increased biofilm formation. In contrast, methylamine inhibited both nitrate reductase and biofilm formation. The correlation between the expression and/or activity or redox enzymes and biofilm-formation activities suggests that these are possible therapeutic targets to erradicate S. epidermidis.

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“…The response regulator NreC is subsequently phosphorylated by NreB and specifically binds to the promoters of the narT gene and of the narGHJI and nirBD operons to activate transcription [ 37 – 39 ]. Since previous studies have shown that both aerobic and anaerobic G3P dehydrogenase can transfer hydrogens from G3P to nitrate, leading to growth of E. coli and S. aureus on glycerol as the carbon source and nitrate as the hydrogen acceptor [ 40 , 41 ]. We speculate the gdpS gene may negatively modulate the entire respiratory pathway consisting of glycerol catabolism and nitrate reduction in S. epidermidis .…”

Section: Resultsmentioning

confidence: 99%

Mutation of gdpS gene induces a viable but non-culturable state in Staphylococcus epidermidis and changes in the global transcriptional profile

Zhu

Wang

et al. 2022

BMC Microbiol

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Background In the genome of staphylococci, only the gdpS gene encodes the conserved GGDEF domain, which is the characteristic of diguanylate cyclases. In our previous study, we have demonstrated that the gdpS gene can modulate biofilm formation by positively regulating the expression of ica operon in Staphylococcus epidermidis. Moreover, this regulation seems to be independent of the c-di-GMP signaling pathway and the protein-coding function of this gene. Therefore, the biological function of the gdpS gene remains to be further investigated. Results In the present study, it was observed that mutation of the gdpS gene induced S. epidermidis to enter into a presumed viable but nonculturable state (VBNC) after cryopreservation with glycerol. Similarly, when moved from liquid to solid culture medium, the gdpS mutant strain also exhibited a VBNC state. Compared with the wild-type strain, the gdpS mutant strain autolyzed more quickly during storage at 4℃, indicating its increased susceptibility to low temperature. Transcriptional profiling analysis showed that the gdpS mutation affected the transcription of 188 genes (92 genes were upregulated and 96 genes were downregulated). Specifically, genes responsible for glycerol metabolism were most markedly upregulated and most of the altered genes in the mutant strain are those involved in nitrogen metabolism. In addition, the most significantly downregulated genes included the betB gene, whose product catalyzes the synthesis of glycine betaine and confers tolerance to cold. Conclusion The preliminary results suggest that the gdpS gene may participate in VBNC formation of S. epidermidis in face of adverse environmental factors, which is probably achieved by regulating expression of energy metabolism genes. Besides, the gdpS gene is critical for S. epidermidis to survive low temperature, and the underlying mechanism may be partly explained by its influence on expression of betB gene.

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sn-Glycerol-3-phosphate dehydrogenase and its interaction with nitrate reductase in wild-type and hem mutant strains of Staphylococcus aureus

Cited by 7 publications

References 14 publications

Proteomic Analysis of Cell Envelope fromStaphylococcusxylosusC2a, a Coagulase-Negative Staphylococcus

Proteomic Analysis of Cell Envelope fromStaphylococcusxylosusC2a, a Coagulase-Negative Staphylococcus

Staphylococcus epidermidis: metabolic adaptation and biofilm formation in response to different oxygen concentrations

Mutation of gdpS gene induces a viable but non-culturable state in Staphylococcus epidermidis and changes in the global transcriptional profile

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