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Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.


ABSTRACT: Here we report the discovery of a bacterial DNA-segregating actin-like protein (BtParM) from Bacillus thuringiensis, which forms novel antiparallel, two-stranded, supercoiled, nonpolar helical filaments, as determined by electron microscopy. The BtParM filament features of supercoiling and forming antiparallel double-strands are unique within the actin fold superfamily, and entirely different to the straight, double-stranded, polar helical filaments of all other known ParMs and of eukaryotic F-actin. The BtParM polymers show dynamic assembly and subsequent disassembly in the presence of ATP. BtParR, the DNA-BtParM linking protein, stimulated ATP hydrolysis/phosphate release by BtParM and paired two supercoiled BtParM filaments to form a cylinder, comprised of four strands with inner and outer diameters of 57 Å and 145 Å, respectively. Thus, in this prokaryote, the actin fold has evolved to produce a filament system with comparable features to the eukaryotic chromosome-segregating microtubule.

SUBMITTER: Jiang S 

PROVIDER: S-EPMC4780641 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.

Jiang Shimin S   Narita Akihiro A   Popp David D   Ghoshdastider Umesh U   Lee Lin Jie LJ   Srinivasan Ramanujam R   Balasubramanian Mohan K MK   Oda Toshiro T   Koh Fujiet F   Larsson Mårten M   Robinson Robert C RC  

Proceedings of the National Academy of Sciences of the United States of America 20160212 9


Here we report the discovery of a bacterial DNA-segregating actin-like protein (BtParM) from Bacillus thuringiensis, which forms novel antiparallel, two-stranded, supercoiled, nonpolar helical filaments, as determined by electron microscopy. The BtParM filament features of supercoiling and forming antiparallel double-strands are unique within the actin fold superfamily, and entirely different to the straight, double-stranded, polar helical filaments of all other known ParMs and of eukaryotic F-a  ...[more]

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