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1991 ◽  
Vol 173 (3) ◽  
pp. 1353-1356 ◽  
Author(s):  
A Macaluso ◽  
A M Mettus
PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16025 ◽  
Author(s):  
Chunying Zhong ◽  
Donghai Peng ◽  
Weixing Ye ◽  
Lujun Chai ◽  
Junliang Qi ◽  
...  

1987 ◽  
Vol 169 (3) ◽  
pp. 1147-1152 ◽  
Author(s):  
A Heierson ◽  
R Landén ◽  
A Lövgren ◽  
G Dalhammar ◽  
H G Boman

Gene ◽  
1982 ◽  
Vol 17 (1) ◽  
pp. 107-112 ◽  
Author(s):  
John D. Reid ◽  
Steven D. Stoufer ◽  
David M. Ogrydziak

1979 ◽  
Vol 76 (10) ◽  
pp. 5259-5263 ◽  
Author(s):  
M. E. Case ◽  
M. Schweizer ◽  
S. R. Kushner ◽  
N. H. Giles

2016 ◽  
Vol 113 (9) ◽  
pp. E1200-E1205 ◽  
Author(s):  
Shimin Jiang ◽  
Akihiro Narita ◽  
David Popp ◽  
Umesh Ghoshdastider ◽  
Lin Jie Lee ◽  
...  

Here we report the discovery of a bacterial DNA-segregating actin-like protein (BtParM) fromBacillus thuringiensis, which forms novel antiparallel, two-stranded, supercoiled, nonpolar helical filaments, as determined by electron microscopy. TheBtParM 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. TheBtParM polymers show dynamic assembly and subsequent disassembly in the presence of ATP.BtParR, the DNA-BtParM linking protein, stimulated ATP hydrolysis/phosphate release byBtParM and paired two supercoiledBtParM 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.


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