5nr1 | pdb_00005nr1
FzlA from C. crescentus
Structural highlights
Publication Abstract from PubMedDuring 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. This article is protected by copyright. All rights reserved. FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.,Lariviere PJ, Szwedziak P, Mahone CR, Lowe J, Goley ED Mol Microbiol. 2017 Nov 9. doi: 10.1111/mmi.13876. PMID:29119622[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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