FtsA forms actin-like protofilaments

被引：166
作者：
Szwedziak, Piotr [1 ]
Wang, Qing [1 ]
Freund, Stefan M. V. [1 ]
Loewe, Jan [1 ]
机构：
[1] MRC Lab Mol Biol, Cambridge 2 0QH, England
来源：
EMBO JOURNAL | 2012年 / 31卷 / 10期
基金：
英国医学研究理事会;
关键词：
actin; bacterial cytoskeleton; cell division; cytomotive; FtsZ; CELL-DIVISION PROTEIN; MEMBRANE TARGETING SEQUENCE; ESCHERICHIA-COLI FTSA; Z-RING; BACILLUS-SUBTILIS; SELF-INTERACTION; ZIPA; LOCALIZATION; BINDING; SEGREGATION;
D O I：
10.1038/emboj.2012.76
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 angstrom. 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. The EMBO Journal (2012) 31, 2249-2260. doi:10.1038/emboj.2012.76; Published online 30 March 2012
引用
收藏
页码：2249 / 2260
页数：12
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