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ARCHAEAL BIOLOGY

It takes two to divide

Nature Reviews Microbiology volume 19, page 405 (2021)Cite this article

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Bacterial cytokinesis is driven by the tubulin homologue FtsZ, which polymerizes into filaments in a GTP-dependent manner to form a ring-like structure termed the Z-ring at the site of division. The Z-ring functions as a platform for the recruitment of numerous other proteins involved in cell division. Archaeal genomes encode multiple ftsZ homologues, but the presence of other cell division proteins remains elusive. The archaeal model organism Haloferax volcanii contains two FtsZ proteins, FtsZ1 and FtsZ2, and in this study, Liao, Ithurbide et al. uncover that FtsZ1 and FtsZ2 have different functions during archaeal cell division.

FtsZ2 functions primarily in the constriction mechanism, and FtsZ1 forms a scaffold to recruit and stabilize the division machinery

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Original article

  • Liao, Y. & Ithurbide, S. et al. Cell division in the archaeon Haloferax volcanii relies on two FtsZ proteins with distinct functions in division ring assembly and constriction. Nat. Microbiol. 6, 594–605 (2021)

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  1. Nature Reviews Microbiology http://www.nature.com/nrmicro/

    Andrea Du Toit

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  1. Andrea Du Toit
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Correspondence to Andrea Du Toit.

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Du Toit, A. It takes two to divide. Nat Rev Microbiol 19, 405 (2021). https://doi.org/10.1038/s41579-021-00568-x

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  • DOI: https://doi.org/10.1038/s41579-021-00568-x

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