title: The tubulin homologue FtsZ contributes to cell elongation by guiding cell wall precursor synthesis in Caulobacter crescentus.
abstract: 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.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, and Microbiology Program, Yale University, New Haven, CT 06520, USA.
authors.forename: Michelle
authors.initials: M
authors.lastname: Aaron
authors.forename: Godefroid
authors.initials: G
authors.lastname: Charbon
authors.forename: Hubert
authors.initials: H
authors.lastname: Lam
authors.forename: Heinz
authors.initials: H
authors.lastname: Schwarz
authors.forename: Waldemar
authors.initials: W
authors.lastname: Vollmer
authors.forename: Christine
authors.initials: C
authors.lastname: Jacobs-Wagner
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000032:analysis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D016935:Caulobacter crescentus / Q000166:cytology / Q000254:growth & development* / Q000378:metabolism; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000032:analysis / Q000378:metabolism*; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D017351:N-Acetylglucosaminyltransferases / Q000032:analysis / Q000378:metabolism*; D016622:Silver Staining; D014538:Uridine Diphosphate N-Acetylmuramic Acid / Q000031:analogs & derivatives* / Q000096:biosynthesis
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D014538:Uridine Diphosphate N-Acetylmuramic Acid; C069249:muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol; D017351:N-Acetylglucosaminyltransferases; C064057:UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase