Toggle Main Menu Toggle Search

Open Access padlockePrints

FtsZ Polymer-bundling by the Escherichia coli ZapA Orthologue, YgfE, Involves a Conformational Change in Bound GTP

Lookup NU author(s): Dr David Scott, Kate Sloan, Dr Stephen Addinall


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Cell division is a fundamental process for both eukaryotic and prokaryotic cells. In bacteria, cell division is driven by a dynamic, ring-shaped, cytoskeletal element (the Z-ring) made up of polymers of the tubulin-like protein FtsZ. It is thought that lateral associations between FtsZ polymers are important for function of the Z-ring in vivo, and that these interactions are regulated by accessory cell division proteins such as ZipA, EzrA and ZapA. We demonstrate that the putative Escherichia coli ZapA orthologue, YgfE, exists in a dimer/tetramer equilibrium in solution, binds to FtsZ polymers, strongly promotes FtsZ polymer bundling and is a potent inhibitor of the FtsZ GTPase activity. We use linear dichroism, a technique that allows structure analysis of molecules within linear polymers, to reveal a specific conformational change in GTP bound to FtsZ polymers, upon bundling by YgfE. We show that the consequences of FtsZ polymer bundling by YgfE and divalent cations are very similar in terms of GTPase activity, bundle morphology and GTP orientation and therefore propose that this conformational change in bound GTP reveals a general mechanism of FtsZ bundling. © 2007 Elsevier Ltd. All rights reserved.

Publication metadata

Author(s): Small E, Marrington R, Rodger A, Scott DJ, Sloan K, Roper D, Dafforn TR, Addinall SG

Publication type: Article

Publication status: Published

Journal: Journal of Molecular Biology

Year: 2007

Volume: 369

Issue: 1

Pages: 210-221

ISSN (print): 0022-2836

ISSN (electronic): 1089-8638

Publisher: Academic Press


DOI: 10.1016/j.jmb.2007.03.025

PubMed id: 17428494


Altmetrics provided by Altmetric


Funder referenceFunder name
G120/738Medical Research Council