Abstract
Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the cytoplasmic membrane. GpsB is a cytosolic protein that affects cell wall synthesis by binding cytoplasmic mini-domains of peptidoglycan synthases to ensure their correct subcellular localisation. Here, we describe critical structural features for the interaction of GpsB with peptidoglycan synthases from three bacterial species (Bacillus subtilis, Listeria monocytogenes and Streptococcus pneumoniae) and suggest their importance for cell wall growth and viability in L. monocytogenes and S. pneumoniae. We use these structural motifs to identify novel partners of GpsB in B. subtilis and extend the members of the GpsB interactome in all three bacterial species. Our results support that GpsB functions as an adaptor protein that mediates the interaction between membrane proteins, scaffolding proteins, signalling proteins and enzymes to generate larger protein complexes at specific sites in a bacterial cell cycle-dependent manner.
Highlights
Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the cytoplasmic membrane
GpsB is an influential cell cycle regulator in low G+C Grampositive bacteria and we set out to establish the common rules by which GpsB interacts with major PG synthases in three important bacteria—one model species (B. subtilis) and two pathogens (L. monocytogenes and S. pneumoniae)
While submicromolar concentrations of BsGpsB bound to chips coated with the wild-type B. subtilis PBP1 (BsPBP1), there was no interaction even when 25 μM BsGpsB was injected over equivalent chips coated with BsPBP117-914 (Fig. 1a)
Summary
Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the cytoplasmic membrane. We describe critical structural features for the interaction of GpsB with peptidoglycan synthases from three bacterial species (Bacillus subtilis, Listeria monocytogenes and Streptococcus pneumoniae) and suggest their importance for cell wall growth and viability in L. monocytogenes and S. pneumoniae. GpsB was initially characterised in Bacillus subtilis where severe cell division and growth defects were observed when both gpsB and ezrA11 or gpsB and ftsA12 were deleted Both EzrA and FtsA play roles in the dynamics and membrane anchoring of the FtsZ Z-ring, the constriction of which is fundamental to cell division[16]. GpsB deletion in L. monocytogenes resulted in enhanced susceptibility to β-lactam[19] and fosfomycin[20] antibiotics, reduced virulence in an insect infection model[19], and caused alterations to PG structure[21]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
