Biosynthesis of teichoic acid inmicrococcus variansATCC 29750 (original) (raw)
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Attachment of the main chain to the linkage unit in biosynthesis of teichoic acids
Journal of Bacteriology, 1981
The main chain of teichoic acids can be assembled in cell-free membrane preparations by the transfer of residues from the appropriate nucleotide precursors to an incompletely characterized amphiphilic molecule, lipoteichoic acid carrier (LTC). However, in the cell wall, the man chain is attached to peptidoglycan through a linkage unit which is synthesized independently. It is believed that, in these cell-free systems, lipid intermediates carrying linkage units are also able to accept residues directly from nucleotide precursors to build up the main chain. In this paper, we have shown that the main chain attached to LTC was transferred from LTC to lipids containing the linkage unit. Thus, in these systems, there appear to be two routes to the biosynthesis of teichoic acid-linkage unit complexes, one by direct assembly of the main chain on linkage unit lipids and the other by transfer of the preassembled main chain from LTC to the linkage unit. It was also shown that linkage unit lipids from different orgnisms were interchangeable and that these were used for polymer synthesis by BaciUus subtilis 3610, in which the teichoic acid is a poly(glycerol phosphate).
Analytical Biochemistry, 2009
The WecA transferase is an integral membrane protein and a member of the polyprenyl phosphate N-acetylhexosamine-1-phosphate transferase superfamily. It initiates the biosynthesis of various bacterial cell envelope components such as the lipopolysaccharide O-antigen. We report on the first large-scale enzymatic synthesis, purification, and characterization of the undecaprenyl-pyrophosphoryl-N-acetylglucosamine product of the WecA transferase. This is an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. Its availability in a pure form will allow the biochemical and structural characterization of the various enzymes requiring it as a substrate for the synthesis of cell wall polymers.
Microbiology, 2000
A method is described for measuring the synthesis of poly(glycerol phosphate) [poly(groP)], the major wall teichoic acid (WTA), lipoteichoic acid (LTA) and phospholipid (P-lipid), through fractionation of [2-3 H]glycerol ([2-3 H]gro)labelled Bacillus subtilis cells. When cultures of certain temperature-sensitive mutants defective in one of several tag genes, encoding enzymes involved in WTA synthesis, were transferred to the restrictive temperature, the synthesis of WTA underwent a specific, immediate, block, while that of LTA or P-lipid proceeded unimpeded. These results, in addition to confirming the role of tag genes, demonstrated, reciprocally, the specificity of the fractionation procedure used to distinguish label in WTA from that in LTA or P-lipid. Results of analysis of other, less severely affected, tag-deficient mutants, as well as of another genetically unrelated mutant developing comparable morphological phenotypes in non-permissive conditions, are discussed in relation to a possible mechanism generating the latter phenotype. Fractionation of B. subtilis 168 cells labelled either with [2-3 H]gro or with [1-14 C]Nacetylglucosamine, to which tunicamycin was added at 05 µg ml N1 (the MIC) revealed a specific and marked inhibition of poly(groP) as well as of poly(3-Oβ-D-glucopyranosyl-N-acetylgalactosamine 1-phosphate), the minor WTA. However, for 60 min at least, the syntheses of PG, LTA and P-lipid were barely affected.
Cytoplasmic steps of peptidoglycan biosynthesis
FEMS Microbiology Reviews, 2008
The biosynthesis of bacterial cell wall peptidoglycan is a complex process that involves enzyme reactions that take place in the cytoplasm (synthesis of the nucleotide precursors) and on the inner side (synthesis of lipid-linked intermediates) and outer side (polymerization reactions) of the cytoplasmic membrane. This review deals with the cytoplasmic steps of peptidoglycan biosynthesis, which can be divided into four sets of reactions that lead to the syntheses of (1) UDP-Nacetylglucosamine from fructose 6-phosphate, (2) UDP-N-acetylmuramic acid from UDP-N-acetylglucosamine, (3) UDP-N-acetylmuramyl-pentapeptide from UDP-N-acetylmuramic acid and (4) D-glutamic acid and dipeptide D-alanyl-Dalanine. Recent data concerning the different enzymes involved are presented. Moreover, special attention is given to (1) the chemical and enzymatic synthesis of the nucleotide precursor substrates that are not commercially available and (2) the search for specific inhibitors that could act as antibacterial compounds.