A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery
0301 basic medicine
Escherichia coli Proteins
Cell Cycle
Membrane Proteins
Peptidoglycan
QH426-470
Actins
Polymerization
3. Good health
03 medical and health sciences
Bacterial Proteins
Cell Wall
Polysaccharides
Genetics
Escherichia coli
Morphogenesis
Penicillin-Binding Proteins
Cytoskeleton
Research Article
Cytokinesis
DOI:
10.1371/journal.pgen.1007726
Publication Date:
2018-10-18T17:30:51Z
AUTHORS (13)
ABSTRACT
Cell elongation in rod-shaped bacteria is mediated by the Rod system, a conserved morphogenic complex that spatially controls cell wall assembly by the glycan polymerase RodA and crosslinking enzyme PBP2. Using Escherichia coli as a model system, we identified a PBP2 variant that promotes Rod system function when essential accessory components of the machinery are inactivated. This PBP2 variant hyperactivates cell wall synthesis in vivo and stimulates the activity of RodA-PBP2 complexes in vitro. Cells with the activated synthase also exhibited enhanced polymerization of the actin-like MreB component of the Rod system. Our results define an activation pathway governing Rod system function in which PBP2 conformation plays a central role in stimulating both glycan polymerization by its partner RodA and the formation of cytoskeletal filaments of MreB to orient cell wall assembly. In light of these results, previously isolated mutations that activate cytokinesis suggest that an analogous pathway may also control cell wall synthesis by the division machinery.
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