Tubulin and its prokaryotic homologue FtsZ: a structural and functional comparison
Tubulin and its prokaryotic homologue FtsZ: a structural and functional comparison
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DOI：
10.3184/003685009x461431
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发表时间：
2009-07-01
期刊：
影响因子：
2.1
通讯作者：
Dyer, Nigel
中科院分区：
文献类型：
--
作者：
Dyer, Nigel
微管是真核细胞骨架的三个主要成分之一，由蛋白质微管蛋白构成。 FtsZ 是原核生物中微管蛋白的紧密结构同源物，在细胞分裂过程中发挥重要的结构作用。本文比较了这两种同系物在体内和体外形成的结构的已知信息，并检验了结构附近的水（特别是微管中的水）可能在其形成和稳定性中发挥重要作用的证据。然后，文章检查了证据，表明该水合层可能有助于我们理解微管蛋白和 FtsZ 形成的结构如何通过相关蛋白质和选定的阳离子来稳定。然后，本文考虑了最近对微管蛋白的电荷分布和偶极矩的研究，并将这项工作扩展到包括 FtsZ 的静电特性。然后检查两种蛋白质之间的静电相似性和差异可能与它们形成的丝状结构的相似性和差异相关的方式。
Microtubules are one of the three primary constituents of the eukaryotic cytoskeleton and are constructed from the protein tubulin. FtsZ is a close structural homologue of tubulin within prokaryotes, and plays an important structural role during cell division. This article compares what is known about the structures that these two homologues are able to form in vivo and in vitro and examines the evidence that the water in the immediate vicinity of the structures, particularly in microtubules, may play an important role in their formation and stability. The article then examines evidence that this hydration layer might help our understanding of how the structures formed by tubulin and FtsZ are stabilised by associated proteins and selected cations. The article then considers recent studies of the charge distribution and dipole moments of tubulin and extends this work to include the electrostatic characteristics of FtsZ. There is then an examination of the ways in which the electrostatic similarities and differences between the two proteins might be related to the similarities and differences in the filamentary structures that they form.