TY - JOUR
T1 - FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division
AU - Lariviere, Patrick J.
AU - Szwedziak, Piotr
AU - Mahone, Christopher R.
AU - Löwe, Jan
AU - Goley, Erin D.
N1 - Funding Information:
We would like to thank the Goley and Xiao labs for helpful discussions. We would particularly like to acknowledge Phil Cox and James Valderrama for their invaluable contributions to the early stages of this work, and Anant Bhargava for helping to streamline the process of single cell image analysis. We also thank the Pincus and Brun labs for assistance with Celltool and MicrobeJ respectively. Finally, we thank the Laub and Manley labs and Aurelia Battesti for providing us with plasmids. Funding for this work was provided by the NIH through R01GM108640 (to E.D.G.) and T32GM007445 (training grant support of P.J.L.) and the Medical Research Council, UK through U105184326 (to J.L.).
Funding Information:
We would like to thank the Goley and Xiao labs for helpful discussions. We would particularly like to acknowledge Phil Cox and James Valderrama for their invaluable contributions to the early stages of this work, and Anant Bhargava for helping to streamline the process of single cell image analysis. We also thank the Pincus and Brun labs for assistance with Cell-tool and MicrobeJ respectively. Finally, we thank the Laub and Manley labs and Aurelia Battesti for providing us with plasmids. Funding for this work was provided by the NIH through R01GM108640 (to E.D.G.) and T32GM007445 (training grant support of P.J.L.) and the Medical Research Council, UK through U105184326 (to J.L.).
Publisher Copyright:
© 2017 John Wiley & Sons Ltd.
PY - 2018/1
Y1 - 2018/1
N2 - During bacterial division, polymers of the tubulin-like GTPase FtsZ assemble at midcell to form the cytokinetic Z-ring, which coordinates peptidoglycan (PG) remodeling and envelope constriction. Curvature of FtsZ filaments promotes membrane deformation in vitro, but its role in division in vivo remains undefined. Inside cells, FtsZ directs PG insertion at the division plane, though it is unclear how FtsZ structure and dynamics are mechanistically coupled to PG metabolism. Here we study FzlA, a division protein that stabilizes highly curved FtsZ filaments, as a tool for assessing the contribution of FtsZ filament curvature to constriction. We show that in Caulobacter crescentus, FzlA must bind to FtsZ for division to occur and that FzlA-mediated FtsZ curvature is correlated with efficient division. We observed that FzlA influences constriction rate, and that this activity is associated with its ability to bind and curve FtsZ polymers. Further, we found that a slowly constricting fzlA mutant strain develops ‘pointy’ poles, suggesting that FzlA influences the relative contributions of radial versus longitudinal PG insertion at the septum. These findings implicate FzlA as a critical coordinator of envelope constriction through its interaction with FtsZ and suggest a functional link between FtsZ curvature and efficient constriction in C. crescentus.
AB - During bacterial division, polymers of the tubulin-like GTPase FtsZ assemble at midcell to form the cytokinetic Z-ring, which coordinates peptidoglycan (PG) remodeling and envelope constriction. Curvature of FtsZ filaments promotes membrane deformation in vitro, but its role in division in vivo remains undefined. Inside cells, FtsZ directs PG insertion at the division plane, though it is unclear how FtsZ structure and dynamics are mechanistically coupled to PG metabolism. Here we study FzlA, a division protein that stabilizes highly curved FtsZ filaments, as a tool for assessing the contribution of FtsZ filament curvature to constriction. We show that in Caulobacter crescentus, FzlA must bind to FtsZ for division to occur and that FzlA-mediated FtsZ curvature is correlated with efficient division. We observed that FzlA influences constriction rate, and that this activity is associated with its ability to bind and curve FtsZ polymers. Further, we found that a slowly constricting fzlA mutant strain develops ‘pointy’ poles, suggesting that FzlA influences the relative contributions of radial versus longitudinal PG insertion at the septum. These findings implicate FzlA as a critical coordinator of envelope constriction through its interaction with FtsZ and suggest a functional link between FtsZ curvature and efficient constriction in C. crescentus.
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U2 - 10.1111/mmi.13876
DO - 10.1111/mmi.13876
M3 - Article
C2 - 29119622
AN - SCOPUS:85036522640
VL - 107
SP - 180
EP - 197
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 2
ER -