TY - JOUR
T1 - Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation
AU - Jiang, Shimin
AU - Narita, Akihiro
AU - Popp, David
AU - Ghoshdastider, Umesh
AU - Lee, Lin Jie
AU - Srinivasan, Ramanujam
AU - Balasubramanian, Mohan K.
AU - Oda, Toshiro
AU - Koh, Fujiet
AU - Larsson, Mårten
AU - Robinson, Robert C.
PY - 2016/3/1
Y1 - 2016/3/1
N2 - 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.
AB - 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.
KW - Actin
KW - Filament
KW - Microtubule
KW - ParM
KW - Plasmid
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U2 - 10.1073/pnas.1600129113
DO - 10.1073/pnas.1600129113
M3 - Article
C2 - 26873105
AN - SCOPUS:84959548073
SN - 0027-8424
VL - 113
SP - E1200-E1205
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 9
ER -