Abstract
Bacteria must maintain the ability to modify and repair the peptidoglycan layer without jeopardising its essential functions in cell shape, cellular integrity and intermolecular interactions. A range of new experimental techniques is bringing an advanced understanding of how bacteria regulate and achieve peptidoglycan synthesis, particularly in respect of the central role played by complexes of Sporulation, Elongation or Division (SEDs) and class B penicillin-binding proteins required for cell division, growth and shape. In this review we highlight relationships implicated by a bioinformatic approach between the outer membrane, cytoskeletal components, periplasmic control proteins, and cell elongation/division proteins to provide further perspective on the interactions of these cell division, growth and shape complexes. We detail the network of protein interactions that assist in the formation of peptidoglycan and highlight the increasingly dynamic and connected set of protein machinery and macrostructures that assist in creating the cell envelope layers in Gram-negative bacteria.
Highlights
Peptidoglycan plays a vital role in the maintenance of cell envelope integrity in bacteria generally, and in Gram-Negative bacteria it acts as a stabilising structure that is attached to both the inner and outer membrane lipid bilayers [1]
Localisation of these complexes presumably ensures that peptidoglycan is synthesized at particular regions for either overall growth or highly specialised growth situations such as cell division (Figure 2D); cell curvature; (Figure 2G) polar growth and maintenance (Figure 2E); as well as flagella associated regions (Figure 2F)
The specialisation of peptidoglycan has been postulated to be driven by pathways that are regulated by local enzyme concentrations and protein: protein interactions
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. This precursor is synthesised in the cytoplasm by sequential enzymatic steps attached to undecaprenyl building block precursor. This precursor is synthesised in the cytoplasm by sequential enzymatic phosphate in the inner membrane [2,4]. The newly formed Lipid II is flipped across the inner membrane and steps attached to undecaprenyl phosphate in the inner membrane [2,4]. The newly formed Lipolymerised into glycan chains by the glycosyltransferase (GT) action of class A bifunctional penicillin-binding proteins pid II is flipped across the inner membrane and polymerised into glycan chains by the glyco(PBPs), Sporulation, Elongation or Division proteins (SEDS) in complex with class B monofunctional PBPs or monofunctional syltransferase (GT). The location of the enzymes required for the synthesis of peptidoglycan and its later
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