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Updated: Aug 25, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
The D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae
Cécile Morlot1, Marjolaine Noirclerc-Savoye, André Zapun
1Laboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale J-P Ebel (CEA/CNRS/UJF, UMR 5075), 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
Abstract:
Bacterial division requires the co-ordination of membrane invagination, driven by the constriction of the FtsZ-ring, and concomitant cell wall synthesis, performed by the high-molecular-weight penicillin-binding proteins (HMW PBPs). Using immunofluorescence techniques, we show in Streptococcus pneumoniae that this co-ordination requires PBP3, a D,D-carboxypeptidase that degrades the substrate of the HMW PBPs. In a mutant deprived of PBP3, the apparent rings of HMW PBPs and that of FtsZ are no longer co-localized. In wild-type cells, PBP3 is absent at the future division site and present over the rest of the cell surface, implying that the localization of the HMW PBPs at mid-cell depends on the availability of their substrate. FtsW, a putative translocase of the substrate of the PBPs, forms an apparent ring that is co-localized with the septal HMW PBPs throughout the cell cycle of wild-type cells. In particular, the constriction of the FtsW-ring occurs after that of the FtsZ-ring, with the same delay as the constriction of the septal PBP-rings. However, in the absence of PBP3, FtsW remains co-localized with FtsZ in contrast to the HMW PBPs. Our work reveals an unexpected complexity in the relationships between the division proteins. The consequences of the absence of PBP3 indicate that the peptidoglycan composition is central to the co-ordination of the division process.
Insights
Bacterial cell division relies on coordinating membrane invagination and cell wall synthesis. PBP3 is crucial for this coordination, ensuring proper localization of high-molecular-weight penicillin-binding proteins (HMW PBPs) during division.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- Bacterial division involves coordinated FtsZ-ring constriction and cell wall synthesis by high-molecular-weight penicillin-binding proteins (HMW PBPs).
- The precise mechanisms coordinating these two essential processes remain incompletely understood.
Purpose of the Study:
- To investigate the role of PBP3 in coordinating bacterial cell division in Streptococcus pneumoniae.
- To elucidate the relationship between PBP3, HMW PBPs, FtsZ, and FtsW localization during cell division.
Main Methods:
- Immunofluorescence microscopy was employed to visualize the localization of key division proteins.
- Analysis of a Streptococcus pneumoniae mutant lacking PBP3 was performed.
Main Results:
- PBP3, a D,D-carboxypeptidase, is essential for the co-localization of HMW PBPs and FtsZ rings during cell division.
- In PBP3-deficient mutants, HMW PBPs fail to localize correctly, disrupting the coordination of cell wall synthesis with FtsZ-ring constriction.
- FtsW localization remains coordinated with FtsZ even in the absence of PBP3, suggesting distinct regulatory roles.
Conclusions:
- Peptidoglycan composition, regulated by PBP3 activity, is central to coordinating bacterial cell division.
- The study reveals unexpected complexity in the interactions among bacterial division proteins.
- PBP3's role highlights the importance of substrate availability in directing HMW PBP localization for proper cell division.
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