and the outer membrane.
Research Aims:
Our goal is to achieve a mechanistic understanding of the divisome—specifically how its components assemble, interact, and function collectively. Crucially, we also aim to reconstitute this system in vitro using liposomes. To do this, we have developed protocols to embed the core divisome complex within liposome membranes. Because the core divisome synthesises the bacterial cell wall on the exterior using the precursor lipid II, we will investigate this extracellular biosynthetic process. Additionally, we plan to incorporate FtsZ-ring components on the inside of the liposomes to direct cell wall synthesis and guide divisome localisation. A key question we seek to answer is whether liposome constriction is driven purely by the FtsZ-ring itself, or if it requires active peptidoglycan synthesis via the core divisome.
Methodology & Impact:
This project leverages an interdisciplinary toolkit spanning molecular biology, protein purification, and state-of-the-art structural biology, including electron cryomicroscopy (cryo-EM) and electron cryotomography (cryo-ET) of both liposomes and intact bacterial cells. Aligned with the LMB’s mission in artificial biology, this research aims to successfully reconstitute liposome division in vitro, establishing foundational principles for downstream biological engineering applications.
Funding Notes
View Website
References
Drobnič, T., Salzer, R., Nierhaus, T., Jiang, M.K.X., Bellini, D., Steindorf, A., Albers, S.-V., Baum, B., Löwe, J., 2026. Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery. Proc Natl Acad Sci U S A 123, e2525941123. https://doi.org/10.1073/pnas.2525941123
Käshammer, L., van den Ent, F., Jeffery, M., Jean, N.L., Hale, V.L., Löwe, J., 2023. Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL. Nat Microbiol 8, 1149–1159. https://doi.org/10.1038/s41564-023-01368-0
Nierhaus, T., McLaughlin, S.H., Bürmann, F., Kureisaite-Ciziene, D., Maslen, S.L., Skehel, J.M., Yu, C.W.H., Freund, S.M.V., Funke, L.F.H., Chin, J.W., Löwe, J., 2022. Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN. Nat Microbiol 7, 1686–1701. https://doi.org/10.1038/s41564-022-01206-9
Nußbaum, P., Kureisaite-Ciziene, D., Bellini, D., van der Does, C., Kojic, M., Taib, N., Yeates, A., Tourte, M., Gribaldo, S., Loose, M., Löwe, J., Albers, S.-V., 2024. Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. Nat Microbiol 9, 698–711. https://doi.org/10.1038/s41564-024-01600-5
Wagstaff, J., Löwe, J., 2018. Prokaryotic cytoskeletons: protein filaments organizing small cells. Nat Rev Microbiol 16, 187–201. https://doi.org/10.1038/nrmicro.2017.153
