Disruption of divisome assembly rescued by FtsN–FtsA interaction in
            <i>Escherichia coli</i>

Pichoff, Sébastien; Du, Shishen; Lutkenhaus, Joe

doi:10.1073/pnas.1806450115

Cited by 58 publications

(70 citation statements)

References 44 publications

(136 reference statements)

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“…This is consistent with ZipA having higher affinity for the CCTP of FtsZ than FtsA as inferred previously (Shen and Lutkenhaus, 2009). Also, the resistance provided by FtsA* is consistent with its ability to stabilize the Z ring due to stronger interactions between FtsA* and the CCTP of FtsZ as well as between FtsN and FtsA* (Du et al, 2016;Pichoff et al, 2018). What is not clear though is why FtsEX or MinC C /MinD, which binds the membrane and the CCTP of FtsZ, cannot function as a membrane anchor for the Z ring when two quite disparate proteins, ZipA and FtsA, can.…”

Section: Discussionsupporting

confidence: 88%

How FtsEX localizes to the Z ring and interacts with FtsA to regulate cell division

Henke

Pichoff

et al. 2019

Molecular Microbiology

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Summary In Escherichia coli, FtsEX, a member of the ABC transporter superfamily, is involved in regulating the assembly and activation of the divisome to couple cell wall synthesis to cell wall hydrolysis at the septum. Genetic studies indicate FtsEX acts on FtsA to begin the recruitment of the downstream division proteins but blocks septal PG synthesis until a signal is received that divisome assembly is complete. However, the details of how FtsEX localizes to the Z ring and how it interacts with FtsA are not clear. Our results show that recruitment of FtsE and FtsX is codependent and suggest that the FtsEX complex is recruited through FtsE interacting with the conserved tail of FtsZ (CCTP), thus adding FtsEX to a growing list of proteins that interacts with the CCTP of FtsZ. Furthermore, we find that the N‐terminus of FtsX is not required for FtsEX localization to the Z ring but is required for its functions in cell division indicating that it interacts with FtsA. Taken together, these results suggest that FtsEX first interacts with FtsZ to localize to the Z ring and then interacts with FtsA to promote divisome assembly and regulate septal PG synthesis.

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Section: Discussionsupporting

confidence: 88%

How FtsEX localizes to the Z ring and interacts with FtsA to regulate cell division

Henke

Pichoff

et al. 2019

Molecular Microbiology

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“…Building on previous analyses of interactions between FtsN, the cytoplasmic division protein FtsA, and the periplasmic division proteins FtsQ, FtsL, and FtsB [18,19,51,58,59], our data suggest a mechanism by which environmental pH modulates size. Under physiological conditions, divisome activation requires the conversion of both FtsA and the septal cell wall synthesis machinery into division competent states [54].…”

Section: Discussionsupporting

confidence: 68%

“…Although our data indicate FtsN is necessary and sufficient for low pH-mediated division activation, it was not clear which regions of FtsN are required for pH-dependent changes in localization. FtsN’s SPOR domain, CCD, and FtsA interaction interface are all believed to influence in its septal localization [49–51]. To clarify which if any of these interactions are pH sensitive, we compared the septal localization frequency of truncations containing both the FtsA interaction interface and CCD (1-105), only the FtsA interaction interface (1-81), or only the SPOR domain (241-319) fused to GFP at low induction levels.…”

Section: Resultsmentioning

confidence: 99%

Environmental pH impacts division assembly and cell size inEscherichia coli

Mueller

Westfall

Levin

2019

Preprint

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Cell size is a complex trait, derived from both genetic and environmental factors. Environmental determinants of bacterial cell size identified to date primarily target assembly of cytosolic components of the cell division machinery. Whether certain environmental cues also impact cell size through changes in the assembly or activity of extracytoplasmic division proteins remains an open question. Here, we identify extracellular pH as a modulator of cell division and a key determinant of cell size across evolutionarily distant bacterial species. In the Gram-negative model organism Escherichia coli, our data indicate environmental pH impacts the length at which cells divide by altering the ability of the terminal cell division protein FtsN to localize to the cytokinetic machinery and activate division. Acidic environments lead to enrichment of FtsN at the septum and activation of division at a reduced cell length, while alkaline pH inhibits FtsN localization and suppress division activation. Altogether, our work reveals a previously unappreciated role for pH in bacterial cell size control.

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“…Indeed, ZipA and FtsA, presumably bound to FtsN, localise at the constriction site until septation is completed 49 , suggesting that this linker function extends from preseptal PG synthesis into septum synthesis. The FtsA–FtsN interaction has recently been shown to promote the recruitment of late cell division proteins and is essential to bypass the absence of FtsEX and FtsK 50 .…”

Section: Discussionmentioning

confidence: 99%

Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division

et al. 2018

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During the transition from elongation to septation, Escherichia coli establishes a ring-like peptidoglycan growth zone at the future division site. This preseptal peptidoglycan synthesis does not require the cell division-specific peptidoglycan transpeptidase PBP3 or most of the other cell division proteins, but it does require FtsZ, its membrane-anchor ZipA and at least one of the bi-functional transglycosylase-transpeptidases, PBP1A or PBP1B. Here we show that PBP1A and PBP1B interact with ZipA and localise to preseptal sites in cells with inhibited PBP3. ZipA stimulates the glycosyltransferase activity of PBP1A. The membrane-anchored cell division protein FtsN localises at preseptal sites and stimulates both activities of PBP1B. Genes zipA and ftsN can be individually deleted in ftsA* mutant cells, but the simultaneous depletion of both proteins is lethal and cells do not establish preseptal sites. Our data support a model according to which ZipA and FtsN-FtsA have semi-redundant roles in connecting the cytosolic FtsZ ring with the membrane-anchored peptidoglycan synthases during the preseptal phase of envelope growth.

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Disruption of divisome assembly rescued by FtsN–FtsA interaction in Escherichia coli

Cited by 58 publications

References 44 publications

How FtsEX localizes to the Z ring and interacts with FtsA to regulate cell division

How FtsEX localizes to the Z ring and interacts with FtsA to regulate cell division

Environmental pH impacts division assembly and cell size inEscherichia coli

Z-ring membrane anchors associate with cell wall synthases to initiate bacterial cell division

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