In vitro reconstitution of Escherichia coli divisome activation

Philipp Radler, Natalia Baranova, Paulo Caldas, Christoph Sommer, Mar López-Pelegrín, David Michalik and Martin Loose ()
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Philipp Radler: Institute for Science and Technology Austria (IST Austria)
Natalia Baranova: Institute for Science and Technology Austria (IST Austria)
Paulo Caldas: Universidade Nova de Lisboa
Christoph Sommer: Institute for Science and Technology Austria (IST Austria)
Mar López-Pelegrín: Institute for Science and Technology Austria (IST Austria)
David Michalik: Institute for Science and Technology Austria (IST Austria)
Martin Loose: Institute for Science and Technology Austria (IST Austria)

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract The actin-homologue FtsA is essential for E. coli cell division, as it links FtsZ filaments in the Z-ring to transmembrane proteins. FtsA is thought to initiate cell constriction by switching from an inactive polymeric to an active monomeric conformation, which recruits downstream proteins and stabilizes the Z-ring. However, direct biochemical evidence for this mechanism is missing. Here, we use reconstitution experiments and quantitative fluorescence microscopy to study divisome activation in vitro. By comparing wild-type FtsA with FtsA R286W, we find that this hyperactive mutant outperforms FtsA WT in replicating FtsZ treadmilling dynamics, FtsZ filament stabilization and recruitment of FtsN. We could attribute these differences to a faster exchange and denser packing of FtsA R286W below FtsZ filaments. Using FRET microscopy, we also find that FtsN binding promotes FtsA self-interaction. We propose that in the active divisome FtsA and FtsN exist as a dynamic copolymer that follows treadmilling filaments of FtsZ.

Date: 2022
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DOI: 10.1038/s41467-022-30301-y

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