Gain‐of‐function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling

Schoenemann, Kara M.; Krupka, Marcin; Rowlett, Veronica W.; Distelhorst, Steven L.; Hu, Bo; Margolin, William

doi:10.1111/mmi.14069

Cited by 34 publications

(39 citation statements)

References 66 publications

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“…Regardless of the mechanism, FtsA is proposed to be in a constriction activation pathway that includes FtsN and the complex formed by FtsQ, FtsL and FtsB (FtsQLB) (Liu et al, 2015;Pichoff et al, 2018). Variants of FtsA and FtsN identified in E. coli are also able to bypass loss of an essential, but γ-proteobacteria-specific, membrane anchor for FtsZ called ZipA that is thought to modulate interactions between FtsA, FtsZ and downstream signaling proteins like FtsN (Geissler et al, 2003;Pichoff et al, 2012Pichoff et al, , 2015Schoenemann et al, 2018) (see poster). FtsN, which contains a sporulation-related repeat (SPOR) domain responsible for recognizing denuded glycans (the result of amidase activity) (Yahashiri et al, 2015), could direct the FtsW-FtsI PG synthetic complex (FtsWI) to locations where new PG material should be incorporated.…”

Section: Assembly and Activation Of The Divisomementioning

confidence: 99%

Bacterial cell division at a glance

Mahone

Goley

2020

Journal of Cell Science

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Bacterial cell division is initiated by the midcell assembly of polymers of the tubulin-like GTPase FtsZ. The FtsZ ring (Z-ring) is a discontinuous structure made of dynamic patches of FtsZ that undergo treadmilling motion. Roughly a dozen additional essential proteins are recruited to the division site by the dynamic Z-ring scaffold and subsequently activate cell wall synthesis to drive cell envelope constriction during division. In this Cell Science at a Glance article and the accompanying poster, we summarize our understanding of the assembly and activation of the bacterial cell division machinery. We introduce polymerization properties of FtsZ and discuss our current knowledge of divisome assembly and activation. We further highlight the intimate relationship between the structure and dynamics of FtsZ and the movement and activity of cell wall synthases at the division site, before concluding with a perspective on the most important open questions on bacterial cell division.

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Section: Assembly and Activation Of The Divisomementioning

confidence: 99%

Bacterial cell division at a glance

Mahone

Goley

2020

Journal of Cell Science

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“…A unifying informational role of ATPase FtsA, which has features in common with ABC-F proteins, should be further explored in-depth, as variants of this protein result in gain of function with alteration of the cell's shape, a behaviour consistent with a role as a MxD. This happens in an ATP-dependent manner, in line with management of information for shaping the cell and controlling to cell division (Schoenemann et al, 2018). FtsA is recruited to a ring of FtsZ proteins that use their GTPase activity for energy-dependent treadmilling, a mechanical activity .…”

Section: Positioning Structures Correctlymentioning

confidence: 99%

Omnipresent Maxwell's demons orchestrate information management in living cells

Boël

Danot

Lorenzo

et al. 2019

Microbial Biotechnology

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Summary The development of synthetic biology calls for accurate understanding of the critical functions that allow construction and operation of a living cell. Besides coding for ubiquitous structures, minimal genomes encode a wealth of functions that dissipate energy in an unanticipated way. Analysis of these functions shows that they are meant to manage information under conditions when discrimination of substrates in a noisy background is preferred over a simple recognition process. We show here that many of these functions, including transporters and the ribosome construction machinery, behave as would behave a material implementation of the information‐managing agent theorized by Maxwell almost 150 years ago and commonly known as Maxwell's demon (MxD). A core gene set encoding these functions belongs to the minimal genome required to allow the construction of an autonomous cell. These MxDs allow the cell to perform computations in an energy‐efficient way that is vastly better than our contemporary computers.

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“…transition from early to late division by acting on the oligomerization states of each other (8,9). Genetic experiments suggest that disruption of the FtsA oligomeric state is important for the recruitment of downstream proteins and activation of division (10,11).…”

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confidence: 99%

Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division

Schoenemann¹,

Vega²,

Margolin³

2020

J Bacteriol

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Bacteria such as Escherichia coli divide by organizing filaments of FtsZ, a tubulin homolog that assembles into dynamic treadmilling membrane-associated protein filaments at the cell midpoint. FtsA and ZipA proteins are required to tether these filaments to the inner face of the cytoplasmic membrane, and loss of either tether is lethal. ZipA from E. coli and other closely related species harbors a long linker region that connects the essential N-terminal transmembrane domain to the C-terminal globular FtsZ-binding domain, and part of this linker includes a P/Q-rich peptide that is predicted to be intrinsically disordered. We found unexpectedly that several large deletions of the ZipA linker region, including the entire P/Q rich peptide, had no effect on cell division under normal conditions. However, we found that the loss of the P/Q region made cells more resistant to excess levels of FtsA and more sensitive to conditions that displaced FtsA from FtsZ. FtsA also harbors a short ∼20-residue peptide linker that connects the main globular domain with the C-terminal amphipathic helix that is important for membrane binding. In analogy with ZipA, deletion of 11 of the central residues in the FtsA linker had little effect on FtsA function in cell division. IMPORTANCE Escherichia coli cells divide using a cytokinetic ring composed of polymers of the tubulin-like FtsZ. To function properly, these polymers must attach to the inner surface of the cytoplasmic membrane via two essential membrane-associated tethers, FtsA and ZipA. Both FtsA and ZipA contain peptide linkers that connect their membrane-binding domains with their FtsZ-binding domains. Although they are presumed to be crucial for cell division activity, the importance of these linkers has not yet been rigorously tested. Here, we show that large segments of these linkers can be removed with few consequences for cell division, although several subtle defects were uncovered. Our results suggest that ZipA, in particular, can function in cell division without an extended linker.

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Gain‐of‐function variants of FtsA form diverse oligomeric structures on lipids and enhance FtsZ protofilament bundling

Cited by 34 publications

References 66 publications

Bacterial cell division at a glance

Bacterial cell division at a glance

Omnipresent Maxwell's demons orchestrate information management in living cells

Peptide Linkers within the Essential FtsZ Membrane Tethers ZipA and FtsA Are Nonessential for Cell Division

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