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首页> 外文期刊>Biochemistry >Rate-Limiting Guanosine 5'-Triphosphate Hydrolysis during Nucleotide Turnover by FtsZ,a Prokaryotic Tubulin Homologue Involved in Bacterial Cell Division
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Rate-Limiting Guanosine 5'-Triphosphate Hydrolysis during Nucleotide Turnover by FtsZ,a Prokaryotic Tubulin Homologue Involved in Bacterial Cell Division

机译：FtsZ，参与细菌细胞分裂的原核微管蛋白同源物在核苷酸转换过程中的限速鸟苷5'-三磷酸水解。

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摘要

FtsZ is a prokaryotic tubulin homologue that polymerizes into a dynamic ring during cell division.GTP binding and hydrolysis provide the energy for FtsZ dynamics.However,the precise role of hydrolysis in polymer assembly and turnover is not understood,limiting our understanding of how FtsZ functions in the cell.Here we investigate GTP hydrolysis during the FtsZ polymerization cycle using several complementalry approaches that avoid technical caveats of previous studies.We find that at steady state approx80% of FtsZ polymer subunits are bound to GTP.In addition,we use pre-steady-state,single turnover assays to directly measure the rate of hydrolysis.Hydrolysis was found to occur at approx 8/min and to be a rate-limiting step in GTP turnover;phosphate release rapidly followed.These results clarify previously conflicting results in the literature and suggest that pure FtsZ polymers,unlike microtubules,may not be able to undergo dynamic instability or to store energy in the polymer for force production.
机译：FtsZ是原核微管蛋白的同系物，在细胞分裂过程中会聚合成一个动态环.GTP结合和水解为FtsZ动力学提供了能量。在这里，我们使用几种互补的方法研究了FtsZ聚合周期中的GTP水解，这些方法避免了先前研究的技术难题。我们发现，在稳态下，约80％的FtsZ聚合物亚基都与GTP结合。稳定，单周转测定直接测量水解速率。发现水解速度约为8 / min，是GTP周转的限速步骤;随后迅速释放出磷酸盐。这些结果澄清了以前的矛盾结果。文献表明，与微管不同，纯FtsZ聚合物可能无法经历动态不稳定性或将能量存储在聚合物中以形成ce生产。

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