FtsA forms actin-like protofilaments.

Article Details

Citation

Szwedziak P, Wang Q, Freund SM, Lowe J

FtsA forms actin-like protofilaments.

EMBO J. 2012 May 16;31(10):2249-60. doi: 10.1038/emboj.2012.76. Epub 2012 Mar 30.

PubMed ID
22473211 [ View in PubMed
]
Abstract

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 A. 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Cell division protein FtsZO08398Details