Abstract
Five essential proteins are known to assemble at the division site of Bacillus subtilis. However, the recruitment of the FtsW homolog is still unclear. Here, we take advantage of spore germination to facilitate the depletion of essential proteins and to study the divisome assembly in the absence of previous division events. We show that, unlike what has been shown for the Escherichia coli divisome, the assembly of FtsW is interdependent with the localization of PBP 2B and FtsL, which are key components of the membrane bound division complex. Interestingly, the Z-ring appeared to disassemble upon prolonged depletion of late division proteins. Nevertheless, we could restore Z-ring formation and constriction by re-inducing FtsW, which suggests that the stability of the Z-ring is stimulated by the assembly of a functional division complex.
Highlights
The division of a bacterial cell requires the coordinated synthesis of new cell membrane and cell wall, and is achieved by a dynamic protein complex known as the divisome (Nanninga, 1991; Errington et al, 2003; Adams and Errington, 2009)
PBP 2B is the transpeptidase that is involved in the synthesis of septal peptidoglycan (Daniel et al, 2000), and FtsW has been assumed to facilitate the transport of cytosolically synthesized Lipid II, the lipid-linked precursor for peptidoglycan synthesis, into the existing cell wall (Mohammadi et al, 2011), there appear to be other transporters (Meeske et al, 2015)
Most of the available information about the role of FtsW is based on studies with the Gram-negative bacterium Escherichia coli, but it has not been shown if the same effects apply to the B. subtilis homolog
Summary
The division of a bacterial cell requires the coordinated synthesis of new cell membrane and cell wall, and is achieved by a dynamic protein complex known as the divisome (Nanninga, 1991; Errington et al, 2003; Adams and Errington, 2009). FtsW is essential in E. coli (Ikeda et al, 1989; Khattar et al, 1994, 1997; Boyle et al, 1997) It belongs to the so-called SEDS family, which comprises polypeptides involved in shape, elongation, division, and sporulation (Errington et al, 2003). Septal Recruitment of FtsW in B. subtilis peptidoglycan precursor lipid II, a hypothesis that was supported by a detailed biochemical study (Mohammadi et al, 2011) Aside of this transport role, FtsW may have a structural role as it is required in E. coli for the recruitment to the division site of the FtsI, the essential cell division specific PBP (denoted PBP 2B in B. subtilis) (Wang et al, 1998; Mercer and Weiss, 2002). We observed that upon prolonged absence of late division proteins, the Z-ring disassembles and, interestingly, we could restore Zring formation and constriction by re-inducing FtsW, which suggests that the stability of the Z-ring is stimulated by the binding of the late division proteins
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