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

Shimin Jiang, Akihiro Narita, David Popp, Umesh Ghoshdastider, Lin Jie Lee, Ramanujam Srinivasan, Mohan K. Balasubramanian, Toshiro Oda, Fujiet Koh, Mårten Larsson, Robert C. Robinson

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)E1200-E1205
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number9
Publication statusPublished - Mar 1 2016
Externally publishedYes


  • Actin
  • Filament
  • Microtubule
  • ParM
  • Plasmid

ASJC Scopus subject areas

  • General


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