Synthesis of peptidoglycan and teichoic acid in Bacillus subtilis: role of the electrochemical proton gradient

Harrington, Charles R.; Baddiley, J.

doi:10.1128/jb.159.3.925-933.1984

Cited by 14 publications

(3 citation statements)

References 45 publications

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“…Commonly, the potassium ionophore valinomycin is used together with K + to abolish ΔΨ. ΔpH is usually dissipated by using low concentrations of nigericin; K + must be present and high concentrations of nigericin must be avoided because electrogenic exchange can occur under those conditions and abolish both components of the PMF [126,127]. Use of both nigericin and valinomycin together, in the presence of K + , or use of a protonophore (CCCP) abolishes both the ΔΨ and ΔpH and serves as a negative control.…”

Section: Determination Of Coupling Stoichiometries-as Exemplified By mentioning

confidence: 99%

Alkaline pH homeostasis in bacteria: New insights

Padan

Bibi

Ito

et al. 2005

Biochimica et Biophysica Acta (BBA) - Biomembranes

673

633

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The capacity of bacteria to survive and grow at alkaline pH values is of widespread importance in the epidemiology of pathogenic bacteria, in remediation and industrial settings, as well as in marine, plant-associated and extremely alkaline ecological niches. Alkali-tolerance and alkaliphily, in turn, strongly depend upon mechanisms for alkaline pH homeostasis, as shown in pH shift experiments and growth experiments in chemostats at different external pH values. Transcriptome and proteome analyses have recently complemented physiological and genetic studies, revealing numerous adaptations that contribute to alkaline pH homeostasis. These include elevated levels of transporters and enzymes that promote proton capture and retention (e.g., the ATP synthase and monovalent cation/proton antiporters), metabolic changes that lead to increased acid production, and changes in the cell surface layers that contribute to cytoplasmic proton retention. Targeted studies over the past decade have followed up the long-recognized importance of monovalent cations in active pH homeostasis. These studies show the centrality of monovalent cation/proton antiporters in this process while microbial genomics provides information about the constellation of such antiporters in individual strains. A comprehensive phylogenetic analysis of both eukaryotic and prokaryotic genome databases has identified orthologs from bacteria to humans that allow better understanding of the specific functions and physiological roles of the antiporters. Detailed information about the properties of multiple antiporters in individual strains is starting to explain how specific monovalent cation/proton antiporters play dominant roles in alkaline pH homeostasis in cells that have several additional antiporters catalyzing ostensibly similar reactions. New insights into the pH-dependent Na(+)/H(+) antiporter NhaA that plays an important role in Escherichia coli have recently emerged from the determination of the structure of NhaA. This review highlights the approaches, major findings and unresolved problems in alkaline pH homeostasis, focusing on the small number of well-characterized alkali-tolerant and extremely alkaliphilic bacteria.

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Section: Determination Of Coupling Stoichiometries-as Exemplified By mentioning

confidence: 99%

Alkaline pH homeostasis in bacteria: New insights

Padan

Bibi

Ito

et al. 2005

Biochimica et Biophysica Acta (BBA) - Biomembranes

673

633

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“…Determinations of radioactivity, protein and nucleotide concentrations and the visualisation of standards on chromatograms were as described [14,171. Descending paper chromatography was performed on Whatman 3MM or no.…”

Section: Materials and Analytical Proceduresmentioning

confidence: 99%

Biosynthesis of wall tiechoic acids in Staphylococcus aureus H, Micrococcus varians and Bacillus subtilis W23

Harrington

Baddiley

1985

European Journal of Biochemistry

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The precursors for linkage unit (LU) synthesis in Staphylococcus aureus H were UDP-GlcNAc, UDP-Nacetylmannosamine (ManNAc) and CDP-glycerol and synthesis was stimulated by ATP. Moraprenol-PPGlcNAc-ManNAc-(glycerol phosphate) -was formed from chemically synthesised nioraprenol-PP-GlcNAc, UDP-ManNAc and CDP-glycerol in the presence of Triton X-100. LU intermediates formed under both conditions served as acceptors for ribitol phosphate residues, from CDP-ribitol, which comprise the main chain. The initial transfer of GlcNAc-I-phosphate from UDP-GlcNAc was very sensitive to tunicamycin whereas the subsequent transfer of ManNAc from UDP-ManNAc was not.Poly(G1cNAc-I -phosphate) and LU synthesis in Micrococcus varians, with endogenous lipid acceptor, UDPGlcNAc and CDP-glycerol, was stimulated by UDP-ManNAc. Synthesis of LU on exogenous moraprenol-PPGlcNAc, with Triton X-100, was dependent on UDP-ManNAc and CDP-glycerol and the intermediates formed served as substrates for polymer synthesis. Membranes from Bacillus subtilis W23 had much lower levels of LU synthesis, but UDP-ManNAc was again required for optimal synthesis in the presence of UDP-GlcNAc and CDPglycerol. Conditions for LU synthesis on exogenous moraprenol-PP-GlcNAc were not found in this organism.LU synthesis on endogenous acceptor in the absence of UDP-ManNAc was explained by contamination of membranes with UDP-GlcNAc 2-epimerase. Under appropriate conditions, low levels of this enzyme were sufficient to convert UDP-GlcNAc into a mixture of UDP-Glc-NAc and UDP-ManNAc and account for LU Structural studies on the ribitol teichoic acids of Staphylococcus aureus H and Bacillus subtilis W23 and the poly-(GlcNAc-1-phosphate) of Micrococcus varians showed that these polymers are covalently attached to the muramic acid of peptidoglycan through a common linkage of (Gro-P),-GlcNAc-1-P [l]. The biosynthesis of teichoic acid and its linkage unit (LU) has been recently reviewed [2]. LU is synthesised from the precursors, UDP-GlcNAc and CDPglycerol, through a series of polyisoprenol pyrophosphate intermediates which have been isolated and characterised [3 -71. In S. uureus membranes, poly(ribito1 phosphate) may

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“…ATP is synthesized inside the cell, whereas lipoteichoic acid seems to be concentrated in the outer layer of the cytoplasmic membrane (21 and references therein). Alanylation of lipoteichoic acid may therefore be a transmembrane process such as has previously been documented for the biosynthesis of teichoic acid (4) and peptidoglycan (13,14) in B. subtilis.…”

Section: Discussionmentioning

confidence: 79%

Maintenance of D-alanine ester substitution of lipoteichoic acid by reesterification in Staphylococcus aureus

Koch¹,

Doker²,

Fischer³

1985

J Bacteriol

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Toluene-treated Staphylococcus aureus cells did not synthesize teichoic acid and lipoteichoic acid under the conditions used. The organism displayed, however, a high capacity of incorporating D-[14C]alanine into previously formed polymers. The reaction was dependent on ATP and enhanced by magnesium ions. The incorporation rate into lipoteichoic acid correlated with the rate of loss of alanine ester which occurred through transfer to teichoic acid and base-catalyzed hydrolysis. At pH 6.5 the loss (20% within 4 h) was completely compensated for by reesterification. At pH 7.5 the loss was 60%, but by accelerated incorporation it was reduced to 10%. Incorporation was also enhanced when the original substitution of lipoteichoic acid was lowered by previous growth of S. aureus at high salt concentration. The newly added alanine was randomly distributed along the poly(glycerophosphate) chain. The decreased alanine substitution of lipoteichoic acid after growth at high salt concentration was shown to result from a direct inhibition of alanine incorporation. Lipoteichoic acid and teichoic acid are widespread membrane and cell wall components of gram-positive bacteria. In many cases both polymers are replaced with D-alanine ester (1, 3, 6). A concomitant decrease of the alanine content of teichoic acid (15) and lipoteichoic acid (10) in Staphylococcus aureus at increasing salt concentrations in the growth medium led us to hypothesize that the incorporation of D-alanine into both polymers may be under the same control. In Lactobacillus casei the incorporation into lipoteichoic acid was shown to occur by a two-step reaction (5, 19): Enzyme + D-alanine + ATP = enzyme alanylAMP + PPa Enzyme alanylAMP + lipoteichoic acid alanyl lipoteichoic acid + AMP + enzyme Recent pulse-chase experiments of growing S. aureus with D-[14C]alanine revealed a rapid turnover of the alanine ester

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Synthesis of peptidoglycan and teichoic acid in Bacillus subtilis: role of the electrochemical proton gradient

Cited by 14 publications

References 45 publications

Alkaline pH homeostasis in bacteria: New insights

Alkaline pH homeostasis in bacteria: New insights

Biosynthesis of wall tiechoic acids in Staphylococcus aureus H, Micrococcus varians and Bacillus subtilis W23

Maintenance of D-alanine ester substitution of lipoteichoic acid by reesterification in Staphylococcus aureus

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