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CetZ tubulin-like proteins control archaeal cell shape

机译:CetZ微管蛋白样蛋白控制古细菌细胞形状

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摘要

Tubulin is a major component of the eukaryotic cytoskeleton, controlling cell shape, structure and dynamics, whereas its bacterial homologue FtsZ establishes the cytokinetic ring that constricts during cell division. How such different roles of tubulin and FtsZ evolved is unknown. Studying Archaea may provide clues as these organisms share characteristics with Eukarya and Bacteria. Here we report the structure and function of proteins from a distinct family related to tubulin and FtsZ, named CetZ, which co-exists with FtsZ in many archaea. CetZ X-ray crystal structures showed the FtsZ/tubulin superfamily fold, and one crystal form contained sheets of protofilaments, suggesting a structural role. However, inactiva-tion of CetZ proteins in Haloferax volcanii did not affect cell division. Instead, CetZ1 was required for differentiation of the irregular plate-shaped cells into a rod-shaped cell type that was essential for normal swimming motility. CetZ1 formed dynamic cytoskeletal structures in vivo, relating to its capacity to remodel the cell envelope and direct rod formation. CetZ2 was also implicated in H. volcanii cell shape control. Our findings expand the known roles of the FtsZ/tubulin superfamily to include archaeal cell shape dynamics, suggesting that a cytoskeletal role might predate eukaryotic cell evolution, and they support the premise that a major function of the microbial rod shape is to facilitate swimming.
机译:微管蛋白是真核细胞骨架的主要组成部分,控制着细胞的形状,结构和动力学,而其细菌同源物FtsZ建立了在细胞分裂过程中收缩的细胞动力学环。微管蛋白和FtsZ的不同作用如何演变尚不清楚。研究古细菌可能会提供线索,因为这些生物与Eukarya和细菌具有共同的特征。在这里,我们报告了与微管蛋白和FtsZ相关的一个独特家族蛋白CetZ的结构和功能,该家族与FtsZ在许多古细菌中共存。 CetZ X射线晶体结构显示FtsZ /微管蛋白超家族折叠,并且一种晶体形式包含片状原丝,表明具有结构性作用。但是,Haloferax volcanii中的CetZ蛋白失活不会影响细胞分裂。取而代之的是,需要CetZ1将不规则的板状细胞分化为正常游泳运动必不可少的杆状细胞。 CetZ1在体内形成动态的细胞骨架结构,与其重塑细胞包膜和直接形成杆有关。 CetZ2也与火山嗜血杆菌细胞形状控制有关。我们的发现将FtsZ /微管蛋白超家族的已知作用扩展到包括古细菌细胞形状动力学,这表明细胞骨架作用可能早于真核细胞进化,并且它们支持微生物棒形状的主要功能是促进游泳的前提。

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  • 来源
    《Nature》 |2015年第7543期|362-365|共4页
  • 作者单位

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK,The ithree institute, University of Technology Sydney, New South Wales 2007, Australia;

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK;

    The ithree institute, University of Technology Sydney, New South Wales 2007, Australia,School of Physics, University of New South Wales, Sydney, New South Wales 2052, Australia;

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK;

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK;

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK,The ithree institute, University of Technology Sydney, New South Wales 2007, Australia;

    The ithree institute, University of Technology Sydney, New South Wales 2007, Australia;

    The ithree institute, University of Technology Sydney, New South Wales 2007, Australia;

    The ithree institute, University of Technology Sydney, New South Wales 2007, Australia;

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK;

    Medical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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