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Cytoskeletal Proteins in Bacteria

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Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

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Related Experiment Video

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Three-dimensional Imaging of Bacterial Cells for Accurate Cellular Representations and Precise Protein Localization

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Published on: October 29, 2019

Bacterial actin MreB assembles in complex with cell shape protein RodZ.

Fusinita van den Ent¹, Christopher M Johnson, Logan Persons

¹MRC Laboratory of Molecular Biology, Cambridge, UK.

The EMBO Journal

|February 20, 2010

Summary

The bacterial actin MreB protein, crucial for cell shape, interacts with RodZ. This interaction, detailed by crystal structure, is vital for maintaining rod-shaped bacteria.

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Area of Science:

Microbiology
Structural Biology
Cell Biology

Background:

Bacterial actin homologue MreB maintains cell shape in non-spherical bacteria.
MreB assembles into helical structures beneath the cytoplasmic membrane.
RodZ, a membrane protein, is essential for MreB assembly and cell shape determination.

Purpose of the Study:

To present the first crystal structure of bacterial actin (MreB) interacting with its natural partner (RodZ).
To elucidate the functional significance of the MreB-RodZ interaction in bacterial cell shape maintenance.

Main Methods:

X-ray crystallography to determine the structure of the MreB-RodZ complex.
In vitro and in vivo analyses using mutant RodZ proteins from Thermotoga maritima and Escherichia coli.

Main Results:

The cytoplasmic helix-turn-helix motif of RodZ directly interacts with both monomeric and filamentous MreB.
The crystal structure of the MreB-RodZ complex was determined.
Mutational analyses confirmed the importance of the MreB-RodZ interaction for bacterial cell shape.

Conclusions:

The MreB-RodZ interaction is critical for bacterial cell shape maintenance, enabling cells to propagate as rods.
This interaction may anchor the bacterial actin cytoskeleton to the membrane, influencing peptidoglycan synthesis.