A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in <i>Caulobacter crescentus</i>

Meier, Elizabeth L.; Razavi, Shiva; Inoue, Takanari; Goley, Erin D.

doi:10.1111/mmi.13388

Cited by 34 publications

(58 citation statements)

References 51 publications

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“…Different proteins are employed to tether FtsZ polymers to the membrane. For example, B. subtilis EMPLOYS SEPF, EZRA and FtsA (Singh et al, 2007;Duman et al, 2013), while Caulobacter crescentus uses FzlC, FtsA and possibly a third protein (Meier et al, 2016). SepF and possibly other proteins are likely the membrane anchors in cyanobacteria and actinobacteria that lack FtsA (Marbouty et al 2009;Gola et al 2015).…”

Section: Ftsz-dependent Divisionmentioning

confidence: 99%

Assembly and activation of the Escherichia coli divisome

Lutkenhaus

2017

Molecular Microbiology

181

202

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Cell division in Escherichia coli is mediated by a large protein complex called the divisome. Most of the divisome proteins have been identified, but how they assemble onto the Z ring scaffold to form the divisome and work together to synthesize the septum is not well understood. In this review, we summarize the latest findings on divisome assembly and activation as well as provide our perspective on how these two processes might be regulated.

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Section: Ftsz-dependent Divisionmentioning

confidence: 99%

Assembly and activation of the Escherichia coli divisome

Lutkenhaus

2017

Molecular Microbiology

181

202

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“…In both A. tumefaciens and C. crescentus, the late arrival of FtsA to the divisome suggests that other proteins contribute to proper tethering of FtsZ to the membrane. In C. crescentus, the FtsZ-binding protein, FzlC, functions as a membrane anchor early during the establishment of the divisome (Goley et al, 2010;Meier et al, 2016). A homolog of FzlC is readily found in the A. tumefaciens genome (Atu2824) and may contribute to the ability of FtsZ-rings to form in the absence of FtsA.…”

Section: Ftsa Is Required For Cell Division But Not Initiation Of Gromentioning

confidence: 99%

Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division

Howell

Aliashkevich

Sundararajan

et al. 2019

Molecular Microbiology

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Summary The mechanisms that restrict peptidoglycan biosynthesis to the pole during elongation and re‐direct peptidoglycan biosynthesis to mid‐cell during cell division in polar‐growing Alphaproteobacteria are largely unknown. Here, we explore the role of early division proteins of Agrobacterium tumefaciens including three FtsZ homologs, FtsA and FtsW in the transition from polar growth to mid‐cell growth and ultimately cell division. Although two of the three FtsZ homologs localize to mid‐cell, exhibit GTPase activity and form co‐polymers, only one, FtsZAT, is required for cell division. We find that FtsZAT is required not only for constriction and cell separation, but also for initiation of peptidoglycan synthesis at mid‐cell and cessation of polar peptidoglycan biosynthesis. Depletion of FtsZAT in A. tumefaciens causes a striking phenotype: cells are extensively branched and accumulate growth active poles through tip splitting events. When cell division is blocked at a later stage by depletion of FtsA or FtsW, polar growth is terminated and ectopic growth poles emerge from mid‐cell. Overall, this work suggests that A. tumefaciens FtsZ makes distinct contributions to the regulation of polar growth and cell division.

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“…In line with this, although FtsA is essential in C. crescentus, it is not necessary for the initiation of constriction (35) and is recruited late to the division site (4,34). There is no homolog of ZipA in C. crescentus; instead, the interaction of the Z-ring with the inner membrane in the first stages of divisome assembly seems to be mediated by other proteins, such as the membrane-associated protein FzlC (36,37). It has been recently proposed that the activation of the divisome also occurs in C. crescentus, since point mutations in FtsW, FtsN, and FtsI cause premature division (38,39).…”

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confidence: 78%

A New Essential Cell Division Protein in Caulobacter crescentus

et al. 2017

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Bacterial cell division is a complex process that relies on a multiprotein complex composed of a core of widely conserved and generally essential proteins and on accessory proteins that vary in number and identity in different bacteria. The assembly of this complex and, particularly, the initiation of constriction are regulated processes that have come under intensive study. In this work, we characterize the function of DipI, a protein conserved in Alphaproteobacteria and Betaproteobacteria that is essential in Caulobacter crescentus. Our results show that DipI is a periplasmic protein that is recruited late to the division site and that it is required for the initiation of constriction. The recruitment of the conserved cell division proteins is not affected by the absence of DipI, but localization of DipI to the division site occurs only after a mature divisome has formed. Yeast two-hybrid analysis showed that DipI strongly interacts with the FtsQLB complex, which has been recently implicated in regulating constriction initiation. A possible role of DipI in this process is discussed.IMPORTANCE Bacterial cell division is a complex process for which most bacterial cells assemble a multiprotein complex that consists of conserved proteins and of accessory proteins that differ among bacterial groups. In this work, we describe a new cell division protein (DipI) present only in a group of bacteria but essential in Caulobacter crescentus. Cells devoid of DipI cannot constrict. Although a mature divisome is required for DipI recruitment, DipI is not needed for recruiting other division proteins. These results, together with the interaction of DipI with a protein complex that has been suggested to regulate cell wall synthesis during division, suggest that DipI may be part of the regulatory mechanism that controls constriction initiation.KEYWORDS Caulobacter crescentus, SH3 domain, bacterial cell division, constriction initiation, divisome B acterial cell division is a complex process involving the action of a multiprotein complex known as the divisome (1, 2). In Escherichia coli, the divisome is composed of approximately 30 proteins that assemble into a complex spanning from the cytoplasm to the outer membrane (OM). Of these proteins, only 12 are essential in E. coli and 11 are widely conserved in other bacteria, suggesting that they constitute the core of the divisome (3, 4). The divisome complex starts assembling when a ring formed by the FtsZ protein is stabilized at the site where division will occur (5, 6). FtsZ is a tubulin-related cytoplasmic protein that is brought near the cytoplasmic membrane through its interactions with the membrane-associated protein FtsA and, in E. coli, the transmembrane protein ZipA (7,8). The FtsZ ring generates a force sufficient to deform lipid membranes and probably drives the constriction of the inner membrane (9, 10). After establishment of the FtsZ ring, the FtsEX complex is recruited through the interaction of FtsE with FtsZ (11). The divisome then expands to the peripla...

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A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus

Cited by 34 publications

References 51 publications

Assembly and activation of the Escherichia coli divisome

Assembly and activation of the Escherichia coli divisome

Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division

A New Essential Cell Division Protein in Caulobacter crescentus

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