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Access through your institution Buy or subscribe 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 This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your
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REFERENCES 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) Article CAS Google Scholar Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Nature Reviews Microbiology
http://www.nature.com/nrmicro/ Andrea Du Toit Authors * Andrea Du Toit View author publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR
Correspondence to Andrea Du Toit. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Du Toit, A. It takes two to divide. _Nat Rev Microbiol_ 19, 405 (2021).
https://doi.org/10.1038/s41579-021-00568-x Download citation * Published: 30 April 2021 * Issue Date: July 2021 * DOI: https://doi.org/10.1038/s41579-021-00568-x SHARE THIS ARTICLE Anyone
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