The Metabolic Enzyme CTP Synthase Forms Cytoskeletal Filaments

Nat Cell Biol. 2010 Aug;12(8):739-46. doi: 10.1038/ncb2087. Epub 2010 Jul 18.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / metabolism*
  • Carbon-Nitrogen Ligases / metabolism*
  • Caulobacter crescentus / enzymology
  • Caulobacter crescentus / metabolism
  • Cytoskeleton / metabolism*
  • Microscopy, Fluorescence
  • Microscopy, Phase-Contrast
  • Protein Binding

Substances

  • Bacterial Proteins
  • Carbon-Nitrogen Ligases
  • CTP synthetase