Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube

Biophysics Reviews
Germán RivasSilvia Zorrilla

Abstract

The division of Escherichia coli is an essential process strictly regulated in time and space. It requires the association of FtsZ with other proteins to assemble a dynamic ring during septation, forming part of the functionally active division machinery, the divisome. FtsZ reversibly interacts with FtsA and ZipA at the cytoplasmic membrane to form a proto-ring, the first molecular assembly of the divisome, which is ultimately joined by the rest of the division-specific proteins. In this review we summarize the quantitative approaches used to study the activity, interactions, and assembly properties of FtsZ under well-defined solution conditions, with the aim of furthering our understanding of how the behavior of FtsZ is controlled by nucleotides and physiological ligands. The modulation of the association and assembly properties of FtsZ by excluded-volume effects, reproducing in part the natural crowded environment in which this protein has evolved to function, will be described. The subsequent studies on the reactivity of FtsZ in membrane-like systems using biochemical, biophysical, and imaging technologies are reported. Finally, we discuss the experimental challenges to be met to achieve construction of the minimum protein s...Continue Reading

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Citations

Jul 16, 2013·The Journal of Biological Chemistry·Víctor M Hernández-RocamoraGermán Rivas
Aug 16, 2013·Environmental Microbiology·Mercedes JiménezGermán Rivas
May 19, 2018·PLoS Biology·Diego A Ramirez-DiazPetra Schwille
Oct 2, 2020·Communications Biology·Elisa GodinoChristophe Danelon

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