Recruitment of the TolA Protein to Cell Constriction Sites in Escherichia coli via Three Separate Mechanisms, and a Critical Role for FtsWI Activity in Recruitment of both TolA and TolQ
Cynthia A. Hale, Logan Persons, Piet A. J. de Boer
Abstract
Cell division (cytokinesis) is a fundamental biological process that is incompletely understood for any organism. Division of bacterial cells relies on a ring-like machinery called the septal ring or divisome that assembles along the circumference of the mother cell at the site where constriction will eventually occur. In the well-studied bacterium Escherichia coli, this machinery contains over 30 distinct proteins. We studied how two such proteins, TolA and TolQ, which also play a role in maintaining the integrity of the outer membrane, are recruited to the machinery. We find that TolA can be recruited by three separate mechanisms and that both proteins rely on the activity of a well-studied cell division enzyme for their recruitment.