Dash-and-Recruit Mechanism Drives Membrane Curvature Recognition by the Small Bacterial Protein SpoVM

Edward Y. Kim, Erin R. Tyndall, Kerwyn Casey Huang, Fang Tian, Kumaran S. Ramamurthi

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


In Bacillus subtilis, sporulation requires that the 26-amino acid protein SpoVM embeds specifically into the forespore membrane, a structure with convex curvature. How this nanometer-sized protein can detect curves on a micrometer scale is not well understood. Here, we report that SpoVM exploits a “dash-and-recruit” mechanism to preferentially accumulate on the forespore. Using time-resolved imaging and flow cytometry, we observe that SpoVM exhibits a faster adsorption rate onto membranes of higher convex curvature. This preferential adsorption is accurately modeled as a two-step process: first, an initial binding event occurs with a faster on rate, then cooperative recruitment of additional SpoVM molecules follows. We demonstrate that both this biochemical process and effective sporulation in vivo require an unstructured and flexible SpoVM N terminus. We propose that this two-pronged strategy of fast adsorption followed by recruitment of subsequent molecules is a general mechanism that allows small proteins to detect subtle curves with a radius 1,000-fold their size. SpoVM is a tiny bacterial protein that preferentially accumulates on micrometer-scale convex membranes by employing a two-pronged strategy: fast curvature-dependent adsorption onto convex membranes followed by recruitment of subsequent SpoVM molecules.

Original languageEnglish (US)
Pages (from-to)518-526.e3
JournalCell Systems
Issue number5
StatePublished - Nov 22 2017

All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine
  • Histology
  • Cell Biology


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