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Analysis of interactions between cell division proteins

Final Activity Report Summary - CELLDIV (Analysis of interactions between cell division proteins)

Cell division is a fundamental process that allows for the separation of one mother cell in two identical daughter cells. This mechanism is essential for the survival of bacteria and is highly regulated in time and space by many factors. Understanding, at the molecular level, the machinery running this key process is crucial to open new opportunities of research, particularly in the antibacterial drug discovery. In this project, we were interested in protein factors recruited in the middle of the cell, which catalysed the constriction of the bacterial cell envelope to lead to the separation in two identical cells. Our aim was to understand how those central factors communicated and interacted to each other.

One phase of the project was focussed on a complex composed of three essential proteins that played a central role in cell division of the gram-negative bacteria Escherichia coli. Using a combination of biochemical, genetic and cytological approaches, we made significant progress in the understanding of this complex and we proposed a model of the interactions between these three essential components and the other proteins involved in the cell division machinery.

In a second phase, I exploited the cell division machinery of escherichia coli to develop a novel genetic assay for studying protein-protein interactions under in vivo conditions. In this approach, called 'E. coli artificial septal targeting', an interaction between two proteins was revealed by an easy detectable phenotype, a fluorescence signal in the middle of the cell. Using this assay, I studied the assembly of cell division proteins from the gram-positive bacteria, bacillus subtilis. This investigation helped to characterise interactions between some essential components involved in cell division and to understand the main difference between gram-positive and gram-negative bacteria cell division mechanisms. This study also demonstrated that this new genetic assay might be an efficient tool for detecting stable protein-protein interactions.