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

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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 set needed to initiate bacterial division, without cells, in a cell-like compartment. This integrated approach, combining quantitative and synthetic strategies, will help to support (or dismiss) conclusions already derived from cellular and molecular analysis and to complete our understanding on how bacterial division works.

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Acknowledgments

GR will always be in debt to Allen Minton for his teachings and advice on many aspects of the scientific process, for his motivation and enthusiasm about science and life in general, and for being so generous with his time and knowledge. It is a real privilege to have such an exceptional maestro, a genuine scholar. Thanks for our friendship. The other authors of this review, particularly BM, share these feelings and are deeply grateful to Allen. His frequent visits to our lab have always been very inspirational and educational for all of us.

We also thank the members of our laboratory contributing to the works here reviewed, and Miguel Vicente (CNB-CSIC) for useful discussions and advice on bacterial division. This work was supported by the Spanish government through grants BIO2008-04478-C03 and BIO2011-28941-C03-03 to GR, and BFU2010-14910 and BIO2011-28941-C03-02 to SZ; by the European Commission through contract HEALTH-F3-2009-223432, by the Human Frontiers Science Program through grant RGP0050/2010-C102, and by Comunidad de Madrid through grant S-BIO-0260/2006 to GR; by the CSIC through grants 200980I186 and 201020I001 to SZ and CA, respectively. BM is a JAE postdoctoral associate from the European Social Fund and the Spanish Consejo Superior de Investigaciones Científicas (CSIC).

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Authors and Affiliations

  1. Centro de Investigaciones Biológicas (CIB), c/Ramiro de Maeztu 9, 28040, Madrid, Spain

    Germán Rivas, Carlos Alfonso, Mercedes Jiménez & Begoña Monterroso

  2. Instituto de Química Física “Rocasolano” (CSIC), c/Serrano 119, 28006, Madrid, Spain

    Silvia Zorrilla

Authors
  1. Germán Rivas
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  2. Carlos Alfonso
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  3. Mercedes Jiménez
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  4. Begoña Monterroso
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  5. Silvia Zorrilla
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Corresponding author

Correspondence to Germán Rivas.

Additional information

Special Issue: Protein-Protein and Protein-Ligand Interactions in Dilute and Crowded Solution Conditions. In Honor of Allen Minton’s 70th Birthday.

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Rivas, G., Alfonso, C., Jiménez, M. et al. Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube. Biophys Rev 5, 63–77 (2013). https://doi.org/10.1007/s12551-013-0115-1

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  • DOI: https://doi.org/10.1007/s12551-013-0115-1

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