The metabolic enzyme CTP synthase forms cytoskeletal filaments.

The metabolic enzyme CTP synthase forms cytoskeletal filaments.
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DOI:
10.1038/ncb2087
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发表时间:
2010-08
影响因子:
21.3
通讯作者:
Gitai, Zemer
Gitai, Zemer
中科院分区:
生物学1区
文献类型:
--
作者:
Ingerson-Mahar, Michael;Briegel, Ariane;Werner, John N.;Jensen, Grant J.;Gitai, Zemer

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纤维形成细胞骨架蛋白是所有细胞的关键组织者。主要的真核细胞骨架家族的细菌同源物现已被发现,但研究表明,还有更多的细胞骨架蛋白仍有待鉴定。在这里,我们证明了代谢酶CTP合酶(CtpS)形成细丝在新月柄杆菌。这些细丝是双功能的,并且独立于CtpS催化活性调节柄杆菌曲率。CtpS的形态发生作用需要其与中间丝新月蛋白的功能相互作用。有趣的是,E. coliCtpS同源物在体内和体外也形成纤维,表明CtpS聚合可能广泛保守。E. coliCtpS可以取代柄杆菌CtpS的酶和形态发生功能,表明柄杆菌已经适应了保守的毒素形成蛋白的次要作用。这些结果暗示CtpS作为细菌细胞骨架的一个新的双功能成员,并建议,本地化和聚合可能是代谢酶的重要属性。
Filament-forming cytoskeletal proteins are key organizers of all cells. Bacterial homologs of the major eukaryotic cytoskeletal families have now been discovered, but studies suggest that yet more cytoskeletal proteins remain to be identified. Here we demonstrate that the metabolic enzyme CTP Synthase (CtpS) forms filaments in Caulobacter crescentus. These filaments are bifunctional and regulate Caulobacter curvature independently of CtpS catalytic activity. The morphogenic role of CtpS requires its functional interaction with the intermediate filament crescentin. Interestingly, the E. coli CtpS homolog 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 Caulobacter CtpS, indicating that Caulobacter 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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