Incorporation of [2-3H]glycerol into cell surface components of Bacillus subtilis 168 and thermosensitive mutants affected in wall teichoic acid synthesis: effect of tunicamycin

Pooley, Harold M.; Karamata, Dimitri

doi:10.1099/00221287-146-4-797

Cited by 24 publications

(23 citation statements)

References 33 publications

(43 reference statements)

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“…Evidence pointing to differences in the septal and cylindrical wall in this strain may be correlated with the differential control of WTA synthesis determined by the regulatory elements of this divergon (328). Growth of strains with temperature-sensitive tag mutations (exception tagE) at the restrictive temperature caused an immediate cessation of WTA synthesis, while the synthesis of LTA and phospholipid was not affected (398,402). In contrast to tagF, no conditional lethal phenotypes were observed for tagE.…”

Section: Pathways Of Lta and Wta Biosynthesismentioning

confidence: 90%

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

Neuhaus

Baddiley

2003

Microbiol Mol Biol Rev

900

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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Section: Pathways Of Lta and Wta Biosynthesismentioning

confidence: 90%

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

Neuhaus

Baddiley

2003

Microbiol Mol Biol Rev

900

1,097

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“…The primary target of tunicamycin in S. aureus is TarO, the first enzyme in the WTA biosynthetic pathway, but there is also a secondary target, MraY (19). Although our screen and follow up validation used tunicamycin concentrations that are two orders of magnitude below those that inhibit MraY, we wanted to confirm key results using a fully genetic approach that did not rely on a small molecule (10).…”

Section: Linkage Analysis Provided Gene-gene Validation Of Compound-genementioning

confidence: 99%

“…1) (10,18,19). To use tunicamycin to comprehensively probe the S. aureus genome for interactions with WTAs, we needed a highly saturated transposon mutant library.…”

Section: Significancementioning

confidence: 99%

Compound-gene interaction mapping reveals distinct roles forStaphylococcus aureusteichoic acids

Maria

Sadaka

Moussa

et al. 2014

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

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Staphylococcus aureus contains two distinct teichoic acid (TA) polymers, lipoteichoic acid (LTA) and wall teichoic acid (WTA), which are proposed to play redundant roles in regulating cell division. To gain insight into the underlying biology of S. aureus TAs, we used a small molecule inhibitor to screen a highly saturated transposon library for cellular factors that become essential when WTA is depleted. We constructed an interaction network connecting WTAs with genes involved in LTA synthesis, peptidoglycan synthesis, surface protein display, and D-alanine cell envelope modifications. Although LTAs and WTAs are synthetically lethal, we report that they do not have the same synthetic interactions with other cell envelope genes. For example, D-alanylation, a tailoring modification of both WTAs and LTAs, becomes essential when the former, but not the latter, are removed. Therefore, D-alanine-tailored LTAs are required for survival when WTAs are absent. Examination of terminal phenotoypes led to the unexpected discovery that cells lacking both LTAs and WTAs lose their ability to form Z rings and can no longer divide. We have concluded that the presence of either LTAs or WTAs on the cell surface is required for initiation of S. aureus cell division, but these polymers act as part of distinct cellular networks.synthetic lethality | TraDIS | Tn-seq

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“…Vancomycin inhibits peptidoglycan biosynthesis by binding to lipid II, which contains a monomeric unit of peptidoglycan, and tunicamycin inhibits the biosynthesis of teichoic acid by inhibiting TagO (17,24,26). The pattern of inhibition curves of vancomycin was similar to caprazamycin B, whereas tunicamycin was similar to CPZEN-45.…”

Section: Mtbmentioning

confidence: 73%

“…However, in B. subtilis 168, glycerol is primarily incorporated into teichoic acid (24). Teichoic acids are polysaccharides or polymers of glycerol phosphate, ribitol phosphate, or sugar phosphates attached to peptidoglycan of the cell wall in many species of Gram-positive bacteria (27), and in the case of B. subtilis 168, the dominant teichoic acid is the polymer of glycerol phosphate (Fig.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of the First Step in Synthesis of the Mycobacterial Cell Wall Core, Catalyzed by the GlcNAc-1-phosphate Transferase WecA, by the Novel Caprazamycin Derivative CPZEN-45

Ishizaki

Hayashi

Inoue

et al. 2013

Journal of Biological Chemistry

113

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Background: Because CPZEN-45 is a promising antituberculous drug candidate, the identification of the target is required. Results: CPZEN-45 inhibits the decaprenyl-phosphate-GlcNAc-1-phosphate transferase of Mycobacterium tuberculosis and the corresponding enzyme of Bacillus subtilis responsible for initiation of cell wall synthesis. Conclusion: CPZEN-45 inhibits a novel target in cell wall assembly. Significance: This study is critical for launching CPZEN-45 and for exploitation toward new antituberculous drugs.

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Incorporation of [2-3H]glycerol into cell surface components of Bacillus subtilis 168 and thermosensitive mutants affected in wall teichoic acid synthesis: effect of tunicamycin

Abstract: However, for 60 min at least, the syntheses of PG, LTA and P-lipid were barely affected.

Cited by 24 publications

References 33 publications

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

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

Compound-gene interaction mapping reveals distinct roles forStaphylococcus aureusteichoic acids

Inhibition of the First Step in Synthesis of the Mycobacterial Cell Wall Core, Catalyzed by the GlcNAc-1-phosphate Transferase WecA, by the Novel Caprazamycin Derivative CPZEN-45

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