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233 results on '"Van Heijenoort, Jean"'

7. The GTPase CpgA is implicated in the deposition of the peptidoglycan sacculus in Bacillus subtilis

Author

Absalon, Cedric, Hamze, Kassem, Blanot, Didier, Frehel, Claude, Carballido-Lopez, Rut, Holland, Barry I., van Heijenoort, Jean, and Seror, Simone J.

Subjects
Bacillus subtilis -- Physiological aspects, Peptidoglycans -- Physiological aspects, Guanosine triphosphatase -- Physiological aspects, Biological sciences
Abstract

Depletion of the Bacillus subtilis GTPase CpgA produces abnormal cell shapes, nonuniform deposition of cell wall, and five- to sixfold accumulation of peptidoglycan precursors. Nevertheless, the inherent structure of the cell wall appeared mostly unchanged. The results are consistent with CpgA being involved in coordinating normal peptidoglycan deposition.

Published
2008

12. Peptidoglycan biosynthesis in Escherichia coli: variations in the metabolism of alanine and D-alanyl-D-alanine

Author

de Roubin, Marie-Renee, Mengin-Lecreulx, Dominique, and van Heijenoort, Jean

Subjects
Bacterial cell walls -- Synthesis, Escherichia coli -- Research, Biological sciences
Abstract

The D-alanyl-D-alanine pathway of peptidoglycan biosynthesis in Escherichia coli was investigated. Cells grown on alanine had higher D-alanyl-D-alanine and UDP-MurNac-pentapeptide pools and alanine racemase activity, but had the same or lower alanine pools compared with that of glucose. D-cycloserine led to depletion of the D-alanyl-D-alanine pool of cells grown on glucose and to lysis which was inhibited by chloramphenicol. The ligase and the D-alanyl-D-alanine-adding activities were the same whatever the growth medium.

Published
1992

22. The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm

Author

Bupp, Keith and Van Heijenoort, Jean

Subjects
Escherichia coli -- Physiological aspects, Peptidoglycans -- Physiological aspects, Transferases -- Physiological aspects, Biological sciences
Abstract

The localization of N-acetylglucosaminyltransferase, the enzyme responsible for the final modification of peptidoglycans in Escherichia coli, is investigated using maxicell spheroplast. Trypsin treatmentof the spheroplast reveal a peripheral location for N-acetylglucosaminyltransferase. The enzyme was demonstrated to be associated with the cytoplasmic phase of the cell membrane. This implies that peptidoglycans are assembled to completion prior to secretion.

Published
1993

29. Expression of the Staphylococcus aureus UDP-N-Acetylmuramoyl- l-Alanyl-d-Glutamate:l-Lysine Ligase in Escherichia coli and Effects on Peptidoglycan Biosynthesis and Cell Growth

Author

Mengin-Lecreulx, Dominique, Falla, Tim, Blanot, Didier, van Heijenoort, Jean, Adams, David J., and Chopra, Ian

Subjects
Staphylococcus aureus, Protein Conformation, Physiology and Metabolism, Lysine, Peptidoglycan, Diaminopimelic Acid, complex mixtures, Recombinant Proteins, carbohydrates (lipids), Bacteriolysis, Cell Wall, Muramic Acids, Escherichia coli, bacteria, Cloning, Molecular, Peptide Synthases, Oligopeptides
Abstract

The monomer units in the Escherichia coli and Staphylococcus aureus cell wall peptidoglycans differ in the nature of the third amino acid in the L-alanyl-gamma-D-glutamyl-X-D-alanyl-D-alanine side chain, where X is meso-diaminopimelic acid or L-lysine, respectively. The murE gene from S. aureus encoding the UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: L-lysine ligase was identified and cloned into plasmid vectors. Induction of its overexpression in E. coli rapidly results in abnormal morphological changes and subsequent cell lysis. A reduction of 28% in the peptidoglycan content was observed in induced cells, and analysis of the peptidoglycan composition and structure showed that ca. 50% of the meso-diaminopimelic acid residues were replaced by L-lysine. Lysine was detected in both monomer and dimer fragments, but the acceptor units from the latter contained exclusively meso-diaminopimelic acid, suggesting that no transpeptidation could occur between the epsilon-amino group of L-lysine and the alpha-carboxyl group of D-alanine. The overall cross-linking of the macromolecule was only slightly decreased. Detection and analysis of meso-diaminopimelic acid- and L-lysine-containing peptidoglycan precursors confirmed the presence of L-lysine in precursors containing amino acids added after the reaction catalyzed by the MurE ligase and provided additional information about the specificity of the enzymes involved in these latter processes.

Published
1999

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