Contribution of peptidoglycan to the binding of metal ions by the cell wall ofBacillus subtilis

Matthews, T H; Doyle, Ronald J.; Streips, Uldis N.

doi:10.1007/bf02603134

Cited by 23 publications

(12 citation statements)

References 20 publications

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“…These results show that calcium has a binding constant of 25 × 10 3 M −1 and a binding capacity of 0.78 µmol/mg for cell wall containing both peptidoglycan and WTA (Matthews, Doyle et al 1979). Peptidoglycan alone was determined to have a binding constant of 18 × 10 3 M −1 and a binding capacity of 0.45 µmol/mg (Matthews, Doyle et al 1979). Although our binding constants are much larger for region I, the binding capacity data are similar to the Matthews et al (Matthews, Doyle et al 1979) report.…”

Section: Discussionmentioning

confidence: 89%

“…It has been reported that peptidoglycan contributes half of the cell’s metal binding capacity by comparing the binding of both cell wall fragments (containing peptidoglycan with covalently bound WTA) and peptidoglycan alone (Matthews, Doyle et al 1979). These results show that calcium has a binding constant of 25 × 10 3 M −1 and a binding capacity of 0.78 µmol/mg for cell wall containing both peptidoglycan and WTA (Matthews, Doyle et al 1979).…”

Section: Discussionmentioning

confidence: 99%

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Revised model of calcium and magnesium binding to the bacterial cell wall

Thomas

Rice

2014

Biometals

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Metals bind to the bacterial cell wall yet the binding mechanisms and affinity constants are not fully understood. The cell wall of gram positive bacteria is characterized by a thick layer of peptidoglycan and anionic teichoic acids anchored in the cytoplasmic membrane (lipoteichoic acid) or covalently bound to the cell wall (wall teichoic acid). The polyphosphate groups of teichoic acid provide one-half of the metal binding sites for calcium and magnesium, contradicting previous reports that calcium binding is 100% dependent on teichoic acid. The remaining binding sites are formed with the carboxyl units of peptidoglycan. In this work we report equilibrium association constants and total metal binding capacities for the interaction of calcium and magnesium ions with the bacterial cell wall. Metal binding is much stronger and previously reported. Curvature of Scatchard plots from the binding data and the resulting two regions of binding affinity suggest the presence of negative cooperative binding, meaning that the binding affinity decreases as more ions become bound to the sample. For Ca2+, Region I has a KA = (1.0 ± 0.2) × 106 M−1 and Region II has a KA = (0.075 ± 0.058) × 106 M−1. For Mg2+, KA1 = (1.5 ± 0.1) × 106 and KA2 = (0.17 ± 0.10) × 106. A binding capacity (η) is reported for both regions. However, since binding is still occurring in Region II, the total binding capacity is denoted by η2, which are 0.70 ± 0.04 µmol/mg and 0.67 ± 0.03 µmol/mg for Ca2+ and Mg2+ respectively. These data contradict the current paradigm of there being a single metal affinity value that is constant over a range of concentrations. We also find that measurement of equilibrium binding constants is highly sample dependent, suggesting a role for diffusion of metals through heterogeneous cell wall fragments. As a result, we are able to reconcile many contradictory theories that describe binding affinity and the binding mode of divalent metal cations.

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Revised model of calcium and magnesium binding to the bacterial cell wall

Thomas

Rice

2014

Biometals

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“…They also bind cations and thus constitute a fraction of the wall-binding capacity (127). From a series of covalent modifications of walls from B. subtilis 168, it was concluded that while both TA and peptidoglycan each contribute sites for binding metal cations, the latter would appear to provide a larger fraction (55,131,324,453). In contrast, Heckels et al (212) found that the WTA provides the larger fraction of anionic binding sites in B. subtilis W23, an organism with poly(Rbo-P) WTA.…”

Section: D-alanyl Esters In the Binding Of Ligandsmentioning

confidence: 99%

A Continuum of Anionic Charge: Structures and Functions ofd-Alanyl-Teichoic Acids in Gram-Positive Bacteria

Neuhaus

Baddiley

2003

Microbiol Mol Biol Rev

901

1,097

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SUMMARY Teichoic acids (TAs) are major wall and membrane components of most gram-positive bacteria. With few exceptions, they are polymers of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and d-alanyl ester residues. Wall TA is attached to peptidoglycan via a linkage unit, whereas lipoteichoic acid is attached to glycolipid intercalated in the membrane. Together with peptidoglycan, these polymers make up a polyanionic matrix that functions in (i) cation homeostasis; (ii) trafficking of ions, nutrients, proteins, and antibiotics; (iii) regulation of autolysins; and (iv) presentation of envelope proteins. The esterification of TAs with d-alanyl esters provides a means of modulating the net anionic charge, determining the cationic binding capacity, and displaying cations in the wall. This review addresses the structures and functions of d-alanyl-TAs, the d-alanylation system encoded by the dlt operon, and the roles of TAs in cell growth. The importance of dlt in the physiology of many organisms is illustrated by the variety of mutant phenotypes. In addition, advances in our understanding of d-alanyl ester function in virulence and host-mediated responses have been made possible through targeted mutagenesis of dlt. Studies of the mechanism of d-alanylation have identified two potential targets of antibacterial action and provided possible screening reactions for designing novel agents targeted to d-alanyl-TA synthesis.

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“…The cell walls of gram-positive bacteria have strong metal-binding properties [2]. Some bacteria also produce extracellular polysaccharide sheaths that bind metals [27]. Binding of the siderophore to a heavy metal dramatically changes the free metal concentration.…”

Section: Introductionmentioning

confidence: 99%

Compensation effect of bacterium containing biofertilizer on the growth ofCucumis sativusL. under Al-stress conditions

Tóth

Lévai

Kovács

et al. 2013

Acta Biologica Hungarica

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2Bacterium containing fertilizer and Al-stress AbstractsBiofertilizers are used to improve soil fertility and plant production in sustainable agriculture.However, their applicability depends on several environmental parameters. The aim of our study was to evaluate the effect of free-living bacteria containing fertilizer on the growth of According to our results the biofertilizer is an alternative nutrient supply for replacing chemical fertilizers because it enhances dry matter production. Biofertilizer usage is also offered under Al polluted environmental conditions. Although, the nutrient solution is a clean system where we can examine the main processes without other effects of natural soils. The soil can modify the results, e.g. the soil born microorganisms affect on nutrient availability, and also can modify the harmful effects of different heavy metals. The understanding of basic processes will help us to know more about the soil behaviour.

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Contribution of peptidoglycan to the binding of metal ions by the cell wall ofBacillus subtilis

Cited by 23 publications

References 20 publications

Revised model of calcium and magnesium binding to the bacterial cell wall

Revised model of calcium and magnesium binding to the bacterial cell wall

A Continuum of Anionic Charge: Structures and Functions ofd-Alanyl-Teichoic Acids in Gram-Positive Bacteria

Compensation effect of bacterium containing biofertilizer on the growth ofCucumis sativusL. under Al-stress conditions

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