Coordinated disassembly of the divisome complex in Escherichia coli

Summary The divisome is the macromolecular complex that carries out cell division in Escherichia coli. Every generation it must be assembled, and then disassembled so that the sequestered proteins can be recycled. Whilst the assembly process has been well studied, virtually nothing is known about the disassembly process. In this study, we have used super‐resolution SIM imaging to monitor pairs of fluorescently tagged divisome proteins as they depart from the division septum. These simple binary comparisons indicated that disassembly occurs in a coordinated process that consists of at least five steps: [FtsZ, ZapA] ⇒ [ZipA, FtsA] ⇒ [FtsL, FtsQ] ⇒ [FtsI, FtsN] ⇒ [FtsN]. This sequence of events is remarkably similar to the assembly process, indicating that disassembly follows a first‐in, first‐out principle. A secondary observation from these binary comparisons was that FtsZ and FtsN formed division rings that were spatially separated throughout the division process. Thus the data indicate that the divisome structure can be visualized as two concentric rings; a proto‐ring containing FtsZ and an FtsN‐ring. The divisome is the macromolecular complex that carries out cell division in E. coli. Every generation it must be assembled, and then disassembled so that the sequestered proteins can be recycled. Our study shows disassembly occurs in a co‐ordinated process that consists of at least five steps. The process is remarkably similar to assembly, indicating that disassembly follows a first‐in, first‐out principle. We also show that the divisome structure is composed of two concentric rings.