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FtsA forms actin-like protofilaments
Article first published online: 30 MAR 2012
Copyright © 2012 European Molecular Biology Organization
The EMBO Journal
Volume 31, Issue 10, pages 2249–2260, May 16, 2012
How to Cite
Szwedziak, P., Wang, Q., Freund, S. M. and Löwe, J. (2012), FtsA forms actin-like protofilaments. The EMBO Journal, 31: 2249–2260. doi: 10.1038/emboj.2012.76
- Issue published online: 16 MAY 2012
- Article first published online: 30 MAR 2012
- Manuscript Accepted: 6 MAR 2012
- Manuscript Received: 9 NOV 2011
- bacterial cytoskeleton;
- cell division;
FtsA is an early component of the Z-ring, the structure that divides most bacteria, formed by tubulin-like FtsZ. FtsA belongs to the actin family of proteins, showing an unusual subdomain architecture. Here we reconstitute the tethering of FtsZ to the membrane via FtsA's C-terminal amphipathic helix in vitro using Thermotoga maritima proteins. A crystal structure of the FtsA:FtsZ interaction reveals 16 amino acids of the FtsZ tail bound to subdomain 2B of FtsA. The same structure and a second crystal form of FtsA reveal that FtsA forms actin-like protofilaments with a repeat of 48 Å. The identical repeat is observed when FtsA is polymerized using a lipid monolayer surface and FtsAs from three organisms form polymers in cells when overexpressed, as observed by electron cryotomography. Mutants that disrupt polymerization also show an elongated cell division phenotype in a temperature-sensitive FtsA background, demonstrating the importance of filament formation for FtsA's function in the Z-ring.