EzrA: a spectrin-like scaffold in the bacterial cell division machinery
Authors:Robert M Cleverley, Richard J Lewis
doi: 10.15698/mic2015.02.187
Volume 2, pp. 59 to 61, published 15/01/2015.
Institute for Cell and Molecular Biosciences, University of Newcastle, Newcastle-upon-Tyne, NE2 4HH, UK.
Keywords:
cytoskeleton, cell division, spectrin, EzrA, crystallography
Corresponding Author(s):
Conflict of interest statement:
The authors declare no conflict of interest.
Please cite this article as:
Robert M Cleverley, Richard J Lewis (2015). EzrA: a spectrin-like scaffold in the bacterial cell division machinery. Microbial Cell 2(2): 59-61.
© 2015 Cleverley and Lewis. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
Much progress has been made in identifying the components of the divisome, the assembly of proteins that undertakes the vital process of cell division in bacteria. However, how the highly interdependent processes on either side of the membrane are coordinated during division is a major unresolved question. How is the degradation and synthesis of the cell wall on the outside of the cell coordinated with cytokinesis and membrane fission, which are driven from the inside of the cell by the tubulin homologue FtsZ? A possible key mediator of such coordination is the membrane protein EzrA, as it interacts both with FtsZ and the penicillin binding proteins (PBPs) that synthesize peptidoglycan. Cleverley et al. [Nature Communications (2014) 5, 5421] have recently solved the crystal structure of the cytoplasmic domain of B. subtilis EzrA, which points to an important scaffolding role for EzrA in the divisome. The structure resembles the eukaryotic, cytoskeletal spectrin proteins, which link actin filaments in the cytoskeleton and also connect the actin cytoskeleton to membrane-bound integrin proteins.