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核苷酸水解在肌动蛋白和微管蛋白聚合中的作用。

Role of nucleotide hydrolysis in the polymerization of actin and tubulin.

作者信息

Carlier M F

机构信息

Laboratoire d'Enzymologie, CNRS 91190 Gif-sur-Yvette, France.

出版信息

Cell Biophys. 1988 Jan-Jun;12:105-17. doi: 10.1007/BF02918353.

DOI:10.1007/BF02918353
PMID:2453274
Abstract

Here is presented a short survey of the main aspects of the involvement of nucleotide hydrolysis in the polymerization of actin and microtubules: 1) XTP hydrolysis is not tightly coupled to the polymerization process; XTP hydrolysis and phosphate release generate an unstable XDP-polymer which is maintained at steady state, in the presence of XTP, by terminal XTP-subunits; this feature can generate patterns of phase transitions of the polymer between stable and unstable conformations; 2) Interactions between subunits are involved in the mechanism of XTP hydrolysis; 3) XTP cleavage on the polymer is followed by the slow release of Pi; the structural and thermodynamic characteristics of the transient XDP-Pi-polymer may play a crucial role in the regulation of the dynamics of microtubules and actin filaments.

摘要

以下是对核苷酸水解参与肌动蛋白和微管聚合主要方面的简要综述

1)XTP水解与聚合过程并非紧密偶联;XTP水解和磷酸释放产生不稳定的XDP-聚合物,在XTP存在下,由末端XTP亚基维持其稳态;此特征可产生聚合物在稳定和不稳定构象之间的相变模式;2)亚基间相互作用参与XTP水解机制;3)聚合物上的XTP裂解后,Pi缓慢释放;瞬时XDP-Pi-聚合物的结构和热力学特性可能在微管和肌动蛋白丝动力学调节中起关键作用。

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Role of nucleotide hydrolysis in the polymerization of actin and tubulin.核苷酸水解在肌动蛋白和微管蛋白聚合中的作用。
Cell Biophys. 1988 Jan-Jun;12:105-17. doi: 10.1007/BF02918353.
2
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本文引用的文献

1
Conformation and assembly characteristics of tubulin and microtubule protein from bovine brain.来自牛脑的微管蛋白和微管蛋白的构象与组装特性。
Biochemistry. 1981 Mar 31;20(7):1924-32. doi: 10.1021/bi00510a031.
2
A rapid filtration assay for analysis of microtubule assembly, disassembly, and steady-state tubulin flux.
Methods Cell Biol. 1982;24:159-69. doi: 10.1016/s0091-679x(08)60653-6.
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Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin.N-(1-芘基)碘乙酰胺标记的F-肌动蛋白的荧光测定研究。肌动蛋白原聚体在聚合时以及与重酶解肌球蛋白结合时的局部结构变化。
产气荚膜梭菌iota毒素通过ADP-核糖基化抑制细胞松弛素D刺激的G-肌动蛋白ATP酶。
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Mechanism of K+-induced actin assembly.钾离子诱导肌动蛋白组装的机制。
J Cell Biol. 1982 Jun;93(3):648-54. doi: 10.1083/jcb.93.3.648.
5
Introductory analysis of the GTP-cap phase-change kinetics at the end of a microtubule.微管末端GTP帽相变动力学的初步分析。
Proc Natl Acad Sci U S A. 1984 Nov;81(21):6728-32. doi: 10.1073/pnas.81.21.6728.
6
Phase changes at the end of a microtubule with a GTP cap.具有GTP帽的微管末端的相变。
Proc Natl Acad Sci U S A. 1984 Sep;81(18):5772-6. doi: 10.1073/pnas.81.18.5772.
7
Use of Monte Carlo calculations in the study of microtubule subunit kinetics.蒙特卡罗计算在微管亚基动力学研究中的应用。
Proc Natl Acad Sci U S A. 1983 Dec;80(24):7520-3. doi: 10.1073/pnas.80.24.7520.
8
Interference of GTP hydrolysis in the mechanism of microtubule assembly: an experimental study.GTP水解对微管组装机制的干扰:一项实验研究。
Proc Natl Acad Sci U S A. 1984 Feb;81(3):771-5. doi: 10.1073/pnas.81.3.771.
9
Steady-state theory of the interference of GTP hydrolysis in the mechanism of microtubule assembly.GTP水解对微管组装机制干扰的稳态理论。
Proc Natl Acad Sci U S A. 1983 Dec;80(23):7234-8. doi: 10.1073/pnas.80.23.7234.
10
Dynamic instability of microtubule growth.微管生长的动态不稳定性。
Nature. 1984;312(5991):237-42. doi: 10.1038/312237a0.