Growth in width and FtsZ ring longitudinal positioning in a gammaproteobacterial symbiont.
Rod-shaped bacteria usually grow in length and place their FtsZ ring and division site at midcell, perpendicular to their long axis [1,2]. Here, we provide morphometric and immunocytochemical evidence that a nematode-associated gammaproteobacterium [3,4] grows in width, sets a constricting FtsZ ring parallel to its long axis, and divides longitudinally by default. Remarkably, the newly described FtsZ ring appears to be not only 90° shifted with respect to model rods, but also elliptical and discontinuous. This reveals an unexpected versatility of the gammaproteobacterial cytokinetic machinery.
University of Vienna, Department of Genetics in Ecology, Althanstrasse 14, 1090 Vienna, Austria.
Nikolaus
N
Leisch
Jolanda
J
Verheul
Niels R
NR
Heindl
Harald R
HR
Gruber-Vodicka
Nika
N
Pende
Tanneke
T
den Blaauwen
Silvia
S
Bulgheresi
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000502:physiology; D029968:Escherichia coli Proteins / Q000378:metabolism; D020563:Gammaproteobacteria / Q000502:physiology*; D009348:Nematoda / Q000166:cytology* / Q000382:microbiology* / Q000502:physiology; D010802:Phylogeny; D013559:Symbiosis
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C071525:FtsZ protein, Bacteria; C093548:MinE protein, E coli; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli