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The metabolic enzyme CTP synthase forms cytoskeletal filaments.

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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Ingerson-Mahar M,Briegel A,Werner JN,Jensen GJ,Gitai Z

doi

10.1038/ncb2087

subject

Has Abstract

pub_date

2010-08-01 00:00:00

pages

739-46

issue

8

eissn

1465-7392

issn

1476-4679

pii

ncb2087

journal_volume

12

pub_type

杂志文章

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