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The metabolic enzyme CTP synthase forms cytoskeletal filaments

Ingerson-Mahar, Michael and Briegel, Ariane and Werner, John N. and Jensen, Grant J. and Gitai, Zemer (2010) The metabolic enzyme CTP synthase forms cytoskeletal filaments. Nature Cell Biology, 12 (8). pp. 739-746. ISSN 1465-7392. PMCID PMC3210567.

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Filament-forming cytoskeletal proteins are essential for the structure and organization of all cells. Bacterial homologues of the major eukaryotic cytoskeletal families have now been discovered, but studies suggest that yet more remain to be identified. We demonstrate that the metabolic enzyme CTP synthase (CtpS) forms filaments in Caulobacter crescentus. CtpS is bifunctional, as the filaments it forms regulate the curvature of C. crescentus cells independently of its catalytic function. The morphogenic role of CtpS requires its functional interaction with the intermediate filament, crescentin (CreS). Interestingly, the Escherichia coli CtpS homologue also forms filaments both in vivo and in vitro, suggesting that CtpS polymerization may be widely conserved. E. coli CtpS can replace the enzymatic and morphogenic functions of C. crescentus CtpS, indicating that C. crescentus has adapted a conserved filament-forming protein for a secondary role. These results implicate CtpS as a novel bifunctional member of the bacterial cytoskeleton and suggest that localization and polymerization may be important properties of metabolic enzymes.

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Briegel, Ariane0000-0003-3733-3725
Jensen, Grant J.0000-0003-1556-4864
Gitai, Zemer0000-0002-3280-6178
Additional Information:© 2010 Macmillan Publishers Limited. Received 19 March 2010; accepted 21 June 2010; published online 18 July 2010. We are grateful to B. Bassler, C. Murphy, E. Klein and K. Cowles for critical reading of the manuscript. We thank M. Cabeen, C. Jacobs-Wagner, J. Williamson, Alison Michaelis and other members of the Gitai lab for reagents and discussions. J.N.W. is supported by a postdoctoral fellowship from the National Institute of Allergy and Infectious Diseases (grant 1F32AI073043–01A1). A.B. and G.J.J. were supported in part by the National Institutes of Health (NIH) grant R01 AI067548, the Howard Hughes Medical Institute, and a gift to Caltech from the Gordon and Betty Moore Foundation. Z.G. is supported by funding from the U.S. Department of Energy Office of Science (Biological and Environmental Research; grant DE-FG02-05ER64136), NIH grant 1DP2OD004389-01, the Human Frontiers Science Program and the Beckman Foundation. Author Contributions: M.J.I. performed all experiments except for the ECT and fLM-ECT experiments, which were performed by A.B. J.N.W. performed the initial screen that identified CtpS as a linearly localized protein. Experiments were conceived by M.J.I., A.B., G.J.J. and Z.G., and the manuscript was written by M.J.I. and Z.G. with significant input from A.B. and G.J.J.
Funding AgencyGrant Number
NIH Postdoctoral Fellowship1F32A1073043-01A1
NIHR01 AI067548
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Department of Energy (DOE)DE-FG02-05ER64136
Human Frontiers Science ProgramUNSPECIFIED
Arnold and Mabel Beckman FoundationUNSPECIFIED
Issue or Number:8
PubMed Central ID:PMC3210567
Record Number:CaltechAUTHORS:20100830-105222501
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:19706
Deposited By: Tony Diaz
Deposited On:15 Sep 2010 19:59
Last Modified:21 Apr 2020 23:32

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