FtsZ-Dependent Elongation of a Coccoid Bacterium.
A mechanistic understanding of the determination and maintenance of the simplest bacterial cell shape, a sphere, remains elusive compared with that of more complex shapes. Cocci seem to lack a dedicated elongation machinery, and a spherical shape has been considered an evolutionary dead-end morphology, as a transition from a spherical to a rod-like shape has never been observed in bacteria. Here we show that a Staphylococcus aureus mutant (M5) expressing the ftsZ(G193D) allele exhibits elongated cells. Molecular dynamics simulations and in vitro studies indicate that FtsZ(G193D) filaments are more twisted and shorter than wild-type filaments. In vivo, M5 cell wall deposition is initiated asymmetrically, only on one side of the cell, and progresses into a helical pattern rather than into a constricting ring as in wild-type cells. This helical pattern of wall insertion leads to elongation, as in rod-shaped cells. Thus, structural flexibility of FtsZ filaments can result in an FtsZ-dependent mechanism for generating elongated cells from cocci.



The mechanisms by which bacteria generate and maintain even the simplest cell shape remain an elusive but fundamental question in microbiology. In the absence of examples of coccus-to-rod transitions, the spherical shape has been suggested to be an evolutionary dead end in morphogenesis. We describe the first observation of the generation of elongated cells from truly spherical cocci, occurring in a Staphylococcus aureus mutant containing a single point mutation in its genome, in the gene encoding the bacterial tubulin homologue FtsZ. We demonstrate that FtsZ-dependent cell elongation is possible, even in the absence of dedicated elongation machinery.
Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
Ana R
AR
Pereira
Department of Bioengineering, Stanford University, Stanford, California, USA.
Jen
J
Hsin
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
Ewa
E
Król
Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
Andreia C
AC
Tavares
MICALIS, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
Pierre
P
Flores
W. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA Department of Molecular Biology and Biotechnology, The Krebs Institute, University of Sheffield, Sheffield, United Kingdom.
Egbert
E
Hoiczyk
Department of Bioengineering, Stanford University, Stanford, California, USA.
Natalie
N
Ng
MICALIS, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
Alex
A
Dajkovic
Department of Biology, Indiana University, Bloomington, Indiana, USA.
Yves V
YV
Brun
Department of Chemistry, Indiana University, Bloomington, Indiana, USA.
Michael S
MS
VanNieuwenhze
Infectious Disease Research, Merck Research Laboratories, Kenilworth, New Jersey, USA.
Terry
T
Roemer
MICALIS, INRA, AgroParisTech, Université Paris-Saclay, Jouy-en-Josas, France.
Rut
R
Carballido-Lopez
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
Dirk-Jan
0000-0002-9439-9168
DJ
Scheffers
Department of Bioengineering, Stanford University, Stanford, California, USA Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, USA.
Kerwyn Casey
KC
Huang
Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal mgpinho@itqb.unl.pt.
Mariana G
MG
Pinho
D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000235:genetics* / Q000378:metabolism*; D008853:Microscopy; D056004:Molecular Dynamics Simulation; D050505:Mutant Proteins / Q000235:genetics* / Q000378:metabolism*; D020125:Mutation, Missense; D011487:Protein Conformation; D013211:Staphylococcus aureus / Q000166:cytology* / Q000235:genetics*
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D050505:Mutant Proteins