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Results for “Teichoic Acids”

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At least 433 records · Page 24Linked to original sources
PubMed1992

CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC).

Assays of CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase (CGPTase) (EC 2.7.8.12) in membranes isolated from Bacillus subtilis 168 wild type and 11 strains bearing conditional lethal thermosensitive mutations in tagB, tagD, or tagF revealed that CGPTase deficiency was associated only with mutant tagF alleles. In vitro, thermosensitivity of CGPTase strongly suggests that the structural gene for this enzyme is tagF. We discuss apparent discrepancies between biochemical evidence favoring a membrane location for TagF and a previous report that suggested a cytoplasmic location based on sequence analysis.

Bacillus subtilis↗
PubMed1976

In vitro system for the synthesis of teichoic acid linked to peptidoglycan.

A crude cell wall preparation from Staphylococcus aureus H prepared by the method of Mirelman and Sharon (1972) was shown to catalyze the synthesis of polyribitol phosphate linked to the cell wall peptidoglycan. The reaction used cytidine diphosphate (CDP)-ribitol as a substrate and in addition required the presence of CDP-glycerol, uridine diphosphate (UDP)-N-acetyl-D-glucosamine, and adenosine triphosphate. Incubation of radioactive CDP-glycerol with the crude cell wall preparation resulted in the transfer of glycerol phosphate residues to the cell wall; this reaction was greatly stimulated by the presence of UDP-N-acetylglucosamine. These data suggest that polyribitol phosphate is linked to the cell wall peptidoglycan by an oligomer contaning N-acetyl-D-glucosamine and glycerol phosphate.

Adenosine Triphosphate↗
PubMed1981

Control of synthesis of wall teichoic acid in phosphate-starved cultures of Bacillus subtilis W23.

CDP-glycerol pyrophosphorylase, CDP-ribitol pyrophosphorylase and poly(ribitol phosphate) synthetase activities have been measured in cultures of Bacillus subtilis W23 as they became phosphate-starved either in batch culture or during changeover from potassium limitation to phosphate limitation in a chemostat. The results indicated that repression of synthesis of all three enzymes occurred at the onset of phosphate starvation and that this was accompanied by inhibition of inactivation of CDP-glycerol pyrophosphorylase and poly(ribitol phosphate) synthetase. These results show that the initial response to phosphate starvation involves more than inhibition of one enzyme as proposed by Glaser and Loewy [Glaser L. and Loewy, A. (1979) J. Biol. Chem. 254, 2184-2186]. Synthesis of both linkage unit and poly(ribitol phosphate) are inhibited independently.

Bacillus subtilis↗
PubMed1979

On the structure of the teichoic acid from the cell wall of Streptomyces antibioticus 39. Localization of the phosphodiester linkages and elucidation of the monomeric units structure by means of 13C-nuclear-magnetic-resonance spectroscopy.

The cell walls of Streptomyces antibioticus 39 contain a glycosylated poly(glycerol phosphate), in which the repeating monomeric unit is O-alpha-D-galactopyranosyl-(1--3)-O-2-acetamido-2-deoxy-beta-D-galactopyranosyl-(1--1)-glycerol monophosphate. The localization of the phosphodiester linkages between hydroxyl groups at positions 2 and 3 of the adjacent glycerol residues and the structure of the glycoside were established by 13C nuclear-magnetic-resonance spectroscopy. The spectral data are also in accordance with the results of the methylation analysis and enzyme degradation of the glycoside.

Carbohydrate Conformation↗
PubMed2006

D-alanyl ester depletion of teichoic acids in Lactobacillus plantarum results in a major modification of lipoteichoic acid composition and cell wall perforations at the septum mediated by the Acm2 autolysin.

The insertional inactivation of the dlt operon from Lactobacillus plantarum NCIMB8826 had a strong impact on lipoteichoic acid (LTA) composition, resulting in a major reduction in D-alanyl ester content. Unexpectedly, mutant LTA showed high levels of glucosylation and were threefold longer than wild-type LTA. The dlt mutation resulted in a reduced growth rate and increased cell lysis during the exponential and stationary growth phases. Microscopy analysis revealed increased cell length, damaged dividing cells, and perforations of the envelope in the septal region. The observed defects in the separation process, cell envelope perforation, and autolysis of the dlt mutant could be partially attributed to the L. plantarum Acm2 peptidoglycan hydrolase.

Alanine↗