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FisB relies on homo-oligomerization and lipid binding to catalyze membrane fission in bacteria
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Hughson, Frederick M., Landajuela, Ane, Braun, Martha, Rodrigues, Christopher D.A., Martínez-Calvo, Alejandro, Doan, Thierry, Horenkamp, Florian, Andronicos, Anna, Shteyn, Vladimir, Williams, Nathan D., Lin, Chenxiang, Wingreen, Ned S., Rudner, David Z. and Karatekin, Erdem (2021) FisB relies on homo-oligomerization and lipid binding to catalyze membrane fission in bacteria. PLoS Biology, 19 (6). e3001314. doi:10.1371/journal.pbio.3001314 ISSN 1545-7885.
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Official URL: http://dx.doi.org/10.1371/journal.pbio.3001314
Abstract
Little is known about mechanisms of membrane fission in bacteria despite their requirement for cytokinesis. The only known dedicated membrane fission machinery in bacteria, fission protein B (FisB), is expressed during sporulation in Bacillus subtilis and is required to release the developing spore into the mother cell cytoplasm. Here, we characterized the requirements for FisB-mediated membrane fission. FisB forms mobile clusters of approximately 12 molecules that give way to an immobile cluster at the engulfment pole containing approximately 40 proteins at the time of membrane fission. Analysis of FisB mutants revealed that binding to acidic lipids and homo-oligomerization are both critical for targeting FisB to the engulfment pole and membrane fission. Experiments using artificial membranes and filamentous cells suggest that FisB does not have an intrinsic ability to sense or induce membrane curvature but can bridge membranes. Finally, modeling suggests that homo-oligomerization and trans-interactions with membranes are sufficient to explain FisB accumulation at the membrane neck that connects the engulfment membrane to the rest of the mother cell membrane during late stages of engulfment. Together, our results show that FisB is a robust and unusual membrane fission protein that relies on homo-oligomerization, lipid binding, and the unique membrane topology generated during engulfment for localization and membrane scission, but surprisingly, not on lipid microdomains, negative-curvature lipids, or curvature sensing.
| Item Type: | Journal Article | ||||||||||||||||||||||||
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| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Membranes (Biology), Membrane proteins, Cytoplasm , Lipids -- Physiological transport , Oligomerization , Bacillus subtilis | ||||||||||||||||||||||||
| Journal or Publication Title: | PLoS Biology | ||||||||||||||||||||||||
| Publisher: | Public Library of Science | ||||||||||||||||||||||||
| ISSN: | 1545-7885 | ||||||||||||||||||||||||
| Official Date: | 29 June 2021 | ||||||||||||||||||||||||
| Dates: |
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| Volume: | 19 | ||||||||||||||||||||||||
| Number: | 6 | ||||||||||||||||||||||||
| Article Number: | e3001314 | ||||||||||||||||||||||||
| DOI: | 10.1371/journal.pbio.3001314 | ||||||||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||||||||
| Date of first compliant deposit: | 21 January 2022 | ||||||||||||||||||||||||
| Date of first compliant Open Access: | 24 January 2022 | ||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
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| Is Part Of: | 1 |
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