FtsA forms actin-like protofilaments.
EMBO J
; 31(10): 2249-60, 2012 May 16.
Article
em En
| MEDLINE
| ID: mdl-22473211
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 FtsAFtsZ 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.
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1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Thermotoga maritima
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article