Two FtsZ proteins orchestrate archaeal cell division through distinct functions in ring assembly and constriction
Posted on: 25 June 2020
Preprint posted on 5 June 2020
Article now published in Nature Microbiology at http://dx.doi.org/10.1038/s41564-021-00894-z
A second FtsZ isoform is recruited to constrict archaea that divide without a cell wall
Selected by Dey Lab
Categories: biochemistry, cell biology, evolutionary biology, microbiology
Gabriel Risa [1] and Gautam Dey [1]
[1] MRC lab for Molecular Cell Biology, UCL, London WC1E 6BT, UK
Context
What are FtsZs?
FtsZs are cytoskeletal proteins belonging to the tubulin superfamily found in bacteria, archaea, and some eukaryotic organelles with bacterial ancestry, e.g. plastids (Figure 1). The superfamily is characterised by its GTPase protein domain, which is critical for the proteins’ ability to dynamically assemble into filaments and drive cell shape changes.
What is the cell biological role of FtsZ in bacteria?
FtsZ plays a key role in the bacterial cell division machinery. It is an essential protein in almost all walled bacteria and among the first to assemble at the division site, where it forms part of the Z-ring machinery responsible for cell division (Du and Lutkenhaus, 2017). During cell division, FtsZ treadmilling directs peptidoglycan septal wall synthesis that drives constriction (Bisson-Filho et al., 2017).
What role does FtsZs play in archaea?
FtsZs and CetZs (an archaea-specific tubulin superfamily protein) are found in several archaea (Figure 1). In contrast to bacteria, where normally only one FtsZ homologue is present, archaea often have two FtsZ homologues and numerous CetZ homologues. Intriguingly, whether an archaeon has one or two FtsZ homologues appears to coincide with whether the archaeon has a firm bacterial-like pseudomurein cell wall or a flexible S-layer, respectively.
The archaeon Haloferax volcanii has a single flexible S-layer, two FtsZ homologues, and six CetZs. None of the CetZ homologues are individually required for division, albeit at least one contributes to cell shape (Hartman et al., 2010, Duggin et al., 2015). This work by Liao, Ithurbide et al. examines the cell division of H. volcanii in the context of FtsZ. Their findings offer new insights into how two FtsZ homologues take on different roles to drive cell division in soft archaea.
Key findings
Genetic perturbations of ftsZ1 and ftsZ2 lead to division defects in H. volcanii
Remarkably and unlike bacteria, H. volcanii cells were able to grow and divide in the absence of one or both ftsZ1 and ftsZ2 genes. Nevertheless, through a series of genetic perturbations, Liao, Ithurbide et al. showed that FtsZ1 is key to cell shape and both FtsZ1 and FtsZ2 are important for the cell division process (Figure 2). Cells expressing only ftsZ1 appeared enlarged and rod-shaped, and overexpressing ftsZ1 led WT and deletion strains to form longer rod-shaped cells. In contrast, cells expressing only ftsZ2 were enlarged but discoid, and overexpressing ftsZ2 led WT cells to become smaller. In the ΔftsZ1 deletion strain, overexpressing ftsZ2 led to a partial reversion to WT morphology. In summary, it seems cells become more elongated the more FtsZ1 there is relative to FtsZ2, and overexpression of FtsZ2 can at least partially rescue the loss of FtsZ1.
FtsZ1 and FtsZ2 collaborate during H. volcanii cell division
The authors expressed fluorescently labelled versions of ftsZ1 and ftsZ2 to observe their localisation and behaviour during cell divisions in WT and deletion strains (Figure 3). This was done at low levels of induction, as high levels of labelled proteins interfered with the division process (more a problem with FtsZ2-FP than FtsZ1-FP). FtsZ1 and FtsZ2 both co-localised at the division site and constricted together. In ΔftsZ2 cells, FtsZ1 appeared in ring-like structures, but these did not constrict. In ΔftsZ1 cells, FtsZ2 appeared in puncta and only rarely in rings. However, in some cases where FtsZ2 did appear in rings, it was also capable of constricting.
The above observations and further in-depth analysis on the degree of localisation interdependence, led the authors to propose that FtsZ1 likely plays a more structural and stabilising role compared to FtsZ2 during cell division. Furthermore, they suggest that FtsZ1 is likely recruited prior to FtsZ2 at the division site and that FtsZ2 is the homologue largely responsible for constriction.
Perspectives
Liao, Ithurbide et al. present here a working model for H. volcanii cell division. In doing so, the authors provide a suitable model organism for the study of how FtsZ mediates division in cells with a flexible S-layer, where cell wall synthesis is unlikely to drive constriction. FtsZ is one of the most conserved division proteins on the planet and therefore of great interest to the scientific community, and this work provides valuable new ground on which to build a greater understanding of its operative principles.
Questions for the authors
See questions and author response below!
References
- Bisson-Filho, A.W., Hsu, Y.P., Squyres, G.R., Kuru, E., Wu, F., Jukes, C., Sun, Y., Dekker, C., Holden, S., VanNieuwenhze, M.S., et al. (2017). Treadmilling by FtsZ filaments drives peptidoglycan synthesis and bacterial cell division. Science 355, 739-743.
- Du, S., and Lutkenhaus, J. (2017). Assembly and activation of the Escherichia coli divisome. Mol Microbiol 105, 177-187.
- Duggin, I.G., Aylett, C.H., Walsh, J.C., Michie, K.A., Wang, Q., Turnbull, L., Dawson, E.M., Harry, E.J., Whitchurch, C.B., Amos, L.A., et al. (2015). CetZ tubulin-like proteins control archaeal cell shape. Nature 519, 362-365.
- Hartman, A.L., Norais, C., Badger, J.H., Delmas, S., Haldenby, S., Madupu, R., Robinson, J., Khouri, H., Ren, Q., Lowe, T.M., et al. (2010). The complete genome sequence of Haloferax volcanii DS2, a model archaeon. PLoS One 5, e9605.
doi: https://doi.org/10.1242/prelights.22237
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