期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 9, 页码 E1200-E1205出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1600129113
关键词
actin; ParM; plasmid; filament; microtubule
资金
- A*STAR in Singapore
- Joint Council Office [12302FG012]
- Mechanobiology Institute
- Temasek Life Science Institute (Singapore)
- Japan Society for the Promotion of Science (JSPS) KAKENHI Grant [14431234]
- Nanyang Technological University
- Biomedical Research Council of the Agency for Science, Technology and Research (A*STAR)
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 angstrom and 145 angstrom, 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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