Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution

Author:

Merino-Salomón Adrián1ORCID,Schneider Jonathan2,Babl Leon1ORCID,Krohn Jan-Hagen13,Sobrinos-Sanguino Marta4,Schäfer Tillman5,Luque-Ortega Juan R.4,Alfonso Carlos6,Jiménez Mercedes6,Jasnin Marion7ORCID,Schwille Petra1ORCID,Rivas Germán6ORCID

Affiliation:

1. Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry

2. Department of Molecular Structural Biology, Max Planck Institute of Biochemistry

3. Exzellenzcluster ORIGINS

4. Molecular Interactions Facility, Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC)

5. Cryo-EM facility, Max Planck Institute of Biochemistry

6. Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC)

7. Helmholtz Pioneer Campus, Helmholtz Munich,

Abstract

In most bacteria, division depends on a cytoskeletal structure, the Z ring, which serves as a scaffold for recruiting additional proteins, with which it forms the machinery responsible for division, the divisome. The detailed architecture of the ring, in particular the mechanisms of assembly, stabilization, and disassembly, are still largely unknown. Here, we highlight the role of FtsZ-associated proteins (Zaps) in stabilizing the Z ring by crosslinking the filaments. Among Zap proteins, ZapD binds the C-terminal domain of FtsZ, which serves as a hub for its regulation. We demonstrate that ZapD crosslinks FtsZ filaments in solution into toroidal structures formed by an arrangement of short, curved filaments. Using cryo-electron tomography combined with biochemical analysis, we reveal the three-dimensional organization of FtsZ within the toroids, shedding light on the crosslinking mechanism by ZapD. In spite of the compositional simplicity of our reconstituted system, the structural organization of the FtsZ polymers by ZapD appears to be compatible with the current model of the Z ring in the bacterial cell.

Publisher

eLife Sciences Publications, Ltd

Reference84 articles.

1. Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery;EcoSal Plus,2021

2. At the Heart of Bacterial Cytokinesis: The Z Ring;Trends Microbiol,2019

3. An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome;Int. J. Mol. Sci,2022

4. Tubulin and FtsZ form a distinct family of GTPases;Nat. Struct. Biol. 1998 56,1998

5. The essential bacterial cell-division protein FtsZ is a GTPase;Nat. 1992 3596392,1992

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