Back to Search
Start Over
Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation.
- Source :
- Proceedings of the National Academy of Sciences of the United States of America; 3/1/2016, Vol. 113 Issue 9, pE1200-E1205, 6p
- Publication Year :
- 2016
-
Abstract
- Here we report the discovery of a bacterial DNA-segregating actinlike protein (BtParM) from Bacillus thuringiensis, which forms novel antiparallel, two-stranded, supercoiled, nonpolar helical filaments, as determined by electronmicroscopy. The BtParMfilament 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 chromosomesegregating microtubule. [ABSTRACT FROM AUTHOR]
- Subjects :
- ACTIN
BACILLUS thuringiensis
DNA
ACTOMYOSIN
PROTEINS
Subjects
Details
- Language :
- English
- ISSN :
- 00278424
- Volume :
- 113
- Issue :
- 9
- Database :
- Complementary Index
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 113481119
- Full Text :
- https://doi.org/10.1073/pnas.1600129113