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A metabolic assembly line in bacteria

Nature Cell Biology volume 12, pages 731–733 (2010)Cite this article

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The bacterial cytoplasm is rich in filament-forming proteins, from homologues of eukaryotic cytoskeletal elements to other scaffolding and segregation proteins. We now learn that even the metabolic enzyme CTP synthase forms cytoplasmic filaments that affect bacterial cell shape.

Bacteria keep surprising us. It was not so long ago that they were thought to be mere bags of chemicals, possessing only the cell wall as a sort of exoskeleton to hold everything together. As it turns out, bacterial cells have a sophisticated internal organization. They possess counterparts of tubulin, actin and intermediate filament proteins, suggesting that a cytoskeleton first evolved in bacteria. Moreover, in recent years the known bacterial filament-forming proteins have expanded beyond the traditional cytoskeleton to include DNA segregators, structural scaffolds and proteins, the function of which are still unknown. On page 739 of this issue, Ingerson-Mahar et al. now show that even a protein doing an everyday biochemical task — making the nucleotide CTP — is organized into a filamentous structure1.

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Figure 1: The recent increase in knowledge about filamentous structures in the cytoplasm of walled bacteria.
Figure 2: Possible purposes of CTP synthase polymerization.

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Authors and Affiliations

  1. Department of Molecular, Matthew T. Cabeen is at Yale University, Cellular & Developmental Biology, New Haven, CT 06511, USA.,

    Matthew T. Cabeen

  2. Department of Molecular, Christine Jacobs Wagner is an HHMI Investigator at Yale University, Cellular & Developmental Biology and at Yale University School of Medicine, Microbial Pathogenesis Section, New Haven, CT 06511, USA.,

    Christine Jacobs-Wagner

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Correspondence to Christine Jacobs-Wagner.

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Cabeen, M., Jacobs-Wagner, C. A metabolic assembly line in bacteria. Nat Cell Biol 12, 731–733 (2010). https://doi.org/10.1038/ncb0810-731

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