The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus

Authors

  • Michelle Aaron,

    1. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
    2. Microbiology Program, Yale University, New Haven, CT 06536, USA.
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  • Godefroid Charbon,

    1. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
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  • Hubert Lam,

    1. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
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    • Present addresses: Department of Medicine, Brigham and Women's Hospital/Harvard Medical School, Boston, MA 02115, USA;

  • Heinz Schwarz,

    1. Max-Planck-Institut für Entwicklungsbiologie, 72076 Tübingen, Germany.
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  • Waldemar Vollmer,

    Corresponding author
    1. Mikrobielle Genetik, Universität Tübingen, 72076 Tübingen, Germany.
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    • Institute for Cell and Molecular Biosciences, University of Newcastle upon Tyne, Newcastle upon Tyne, NE2 4HH, UK.

  • Christine Jacobs-Wagner

    Corresponding author
    1. Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
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*E-mail chistine.jacobs-wagner@yale.edu; Tel. (+1) 203 432 5170; Fax (+1) 203 432 6161; E-mail W.Vollmer@ncl.ac.uk; Tel. (+44) 191 2226295; Fax (+44) 191 222 7424.

Summary

The tubulin homologue FtsZ is well known for its essential function in bacterial cell division. Here, we show that in Caulobacter crescentus, FtsZ also plays a major role in cell elongation by spatially regulating the location of MurG, which produces the essential lipid II peptidoglycan cell wall precursor. The early assembly of FtsZ into a highly mobile ring-like structure during cell elongation is quickly followed by the recruitment of MurG and a major redirection of peptidoglycan precursor synthesis to the midcell region. These FtsZ-dependent events occur well before cell constriction and contribute to cell elongation. In the absence of FtsZ, MurG fails to accumulate near midcell and cell elongation proceeds unperturbed in appearance by insertion of peptidoglycan material along the entire sidewalls. Evidence suggests that bacteria use both a FtsZ-independent and a FtsZ-dependent mode of peptidoglycan synthesis to elongate, the importance of each mode depending on the timing of FtsZ assembly during elongation.

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