Probing the Catalytic Activity of a Cell Division-Specific Transpeptidase In Vivo with ß-Lactams

Eberhardt, Christian, Kuerschner, Lars and Weiss, David S. (2003) Probing the Catalytic Activity of a Cell Division-Specific Transpeptidase In Vivo with ß-Lactams. Journal of Bacteriology, 185 13: 3726-3734. doi:10.1128/JB.185.13.3726-3734.2003

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Author Eberhardt, Christian
Kuerschner, Lars
Weiss, David S.
Title Probing the Catalytic Activity of a Cell Division-Specific Transpeptidase In Vivo with ß-Lactams
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1098-5530
Publication date 2003-07
Year available 2003
Sub-type Article (original research)
DOI 10.1128/JB.185.13.3726-3734.2003
Open Access Status File (Publisher version)
Volume 185
Issue 13
Start page 3726
End page 3734
Total pages 9
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2003
Language eng
Abstract Penicillin-binding protein 3 (PBP3; also called FtsI) is a transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall in the division septum of Escherichia coli. To determine whether the catalytic activity of PBP3 is activated during division, we assayed acylation of PBP3 with three ß-lactams (cephalexin, aztreonam, and piperacillin) in growing cells. Acylation of PBP3 with cephalexin, but not aztreonam or piperacillin, appeared to be stimulated by cell division. Specifically, cephalexin acylated PBP3 about 50% faster in a population of dividing cells than in a population of filamentous cells in which division was inhibited by inactivation or depletion of FtsZ, FtsA, FtsQ, FtsW, or FtsN. However, in a simpler in vitro system using isolated membranes, acylation with cephalexin was not impaired by depletion of FtsW or FtsN. A conflicting previous report that the ftsA3(Ts) allele interferes with acylation of PBP3 was found to be due to the presence of a thermolabile PBP3 in the strain used in that study. The new findings presented here are discussed in light of the hypothesis that the catalytic activity of PBP3 is stimulated by interaction(s) with other division proteins. We suggest that there might be allosteric activation of substrate binding
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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