RT Journal Article
SR Electronic
T1 A polymerisation-associated conformational switch in FtsZ that enables treadmilling
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 093708
DO 10.1101/093708
A1 James M. Wagstaff
A1 Matthew Tsim
A1 María A. Oliva
A1 Alba García-Sanchez
A1 Danguole Kureisaite-Ciziene
A1 José Manuel Andreu
A1 Jan Löwe
YR 2016
UL http://biorxiv.org/content/early/2016/12/13/093708.abstract
AB Bacterial cell division in many organisms involves a constricting cytokinetic ring that is orchestrated by the tubulin-like protein FtsZ. FtsZ forms dynamic filaments close to the membrane at the site of division that have recently been shown to treadmill around the division ring, guiding septal wall synthesis.Here, using X-ray crystallography of Staphylococcus aureus SaFtsZ we reveal how an FtsZ can adopt two functionally distinct conformations, open and closed. The open form is found in SaFtsZ filaments formed in crystals and also in soluble filaments of E. coli FtsZ as deduced by cryoEM. The closed form is found within several crystal forms of two non-polymerising SaFtsZ mutants and corresponds to many previous FtsZ structures from other organisms.We argue that FtsZ undergoes a polymerisation-associated conformational switch. We show that such a switch provides explanations for both how treadmilling may occur within a single-stranded filament, and why filament assembly is cooperative.