Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Joachim-Volker Höltje"'
Publikováno v:
Molecular microbiology. 95(4)
Publikováno v:
Journal of Bacteriology. 185:1147-1152
Some strains of Escherichia coli defective for dacA , the gene coding for penicillin-binding protein 5, exhibit a strong branching phenotype when cell division is blocked. Since such branch formation implies a differentiation of polar caps at ectopic
Autor:
Robert A. Nicholas, Lucia Baldi, Joachim Volker Höltje, Silvana Savino, Beatrice Aricò, Guido Grandi, Rino Rappuoli, Astrid Ursinus, Thomas Kast, Gary T. Jennings, Elisa Marchetti
Publikováno v:
European Journal of Biochemistry. 269:3722-3731
In a previous study, we used the genome of serogroup B Meningococcus to identify novel vaccine candidates. One of these molecules, GNA33, is well conserved among Meningococcus B strains, other Meningococcus serogroups and Gonococcus and induces bacte
Publikováno v:
Microbiology. 148:79-86
Periodic activation of zonal peptidoglycan (murein) synthesis at division sites in Escherichia coli has been reported recently. Zonal synthesis is responsible for septum formation, whereas elongation of the cell sacculus is performed by diffuse inser
Autor:
Astrid Ursinus, Miguel A. de Pedro, Christoph Heidrich, Heinz Schwarz, Markus F. Templin, Joachim-Volker Höltje, Jürgen Berger, Melisa Merdanovic
Publikováno v:
Molecular Microbiology. 41:167-178
N-acetylmuramyl-L-alanine amidases are widely distributed among bacteria. However, in Escherichia coli, only one periplasmic amidase has been described until now, which is suggested to play a role in murein recycling. Here, we report that three amida
Publikováno v:
Biochimie. 83:103-108
Multiple deletions in murein hydrolases revealed that predominantly amidases are responsible for cleavage of the septum during cell division. Endopeptidases and lytic transglycosylases seem also be involved. In the absence of these enzymes E. coli gr
Publikováno v:
FEMS Microbiology Letters. 189:201-204
The penicillin-binding proteins PBP 1A and 1Bs are the essential murein polymerases of Escherichia coli. Purification of these membrane-bound bifunctional transglycosylase-transpeptidases was a major obstacle in studying the details of both enzymatic
Publikováno v:
Antimicrobial Agents and Chemotherapy. 44:1181-1185
A simple assay for detection of compounds that bind to the active site in the transglycosylation domain of the essential bifunctional transglycosylase and transpeptidase penicillin-binding proteins (PBPs) is reported. The method is based on a competi
Publikováno v:
Journal of Bacteriology. 181:7192-7198
Physiological studies of a mutant of Escherichia coli lacking the three lytic transglycosylases Slt70, MltA, and MltB revealed that interference with murein turnover can prevent AmpC β-lactamase induction. The triple mutant, although growing normall
Publikováno v:
The EMBO Journal. 18:4108-4117
The first gene of a family of prokaryotic proteases with a specificity for l,d‐configured peptide bonds has been identified in Escherichia coli . The gene named ldcA encodes a cytoplasmic l,d‐carboxypeptidase, which releases the terminal d‐alan