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A Polymerization-Associated Structural Switch in FtsZ That Enables Treadmilling of Model Filaments

DOI: 10.1128/mBio.00254-17 DOI Help

Authors: James Wagstaff (MRC Laboratory of Molecular Biology) , Matthew Tsim (MRC Laboratory of Molecular Biology) , María A. Oliva (CSIC) , Alba García-sanchez (CSIC) , Danguole Kureisaite-ciziene (MRC Laboratory of Molecular Biology) , José Manuel Andreu (CSIC) , Jan Lowe (MRC Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Mbio , VOL 8

State: Published (Approved)
Published: May 2017
Diamond Proposal Number(s): 15916

Open Access Open Access

Abstract: 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 FtsZ (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 Escherichia coli FtsZ as deduced by electron cryomicroscopy. The closed form is found within several crystal forms of two nonpolymerizing SaFtsZ mutants and corresponds to many previous FtsZ structures from other organisms. We argue that FtsZ’s conformational switch is polymerization-associated, driven by the formation of the longitudinal intersubunit interfaces along the filament. 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.

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: European Synchrotron Radiation Facility

Documents:
mBio-2017-Wagstaff-.pdf

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