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了解细胞如何利用金属传感器和金属伴侣蛋白分配金属。

Understanding how cells allocate metals using metal sensors and metallochaperones.

作者信息

Tottey Stephen, Harvie Duncan R, Robinson Nigel J

机构信息

Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle, NE2 4HH, United Kingdom.

出版信息

Acc Chem Res. 2005 Oct;38(10):775-83. doi: 10.1021/ar0300118.

Abstract

Each metalloprotein must somehow acquire the correct metal. We review the insights into metal specificity in cells provided by studies of ArsR-SmtB DNA binding, metal-responsive transcriptional repressors, and a bacterial copper chaperone. Cyanobacteria are the one bacterial group that have known enzymatic demand for cytoplasmic copper import. The copper chaperone and ATPases that supply cyanobacterial plastocyanin and cytochrome oxidase are reviewed, along with related ATPases for cobalt and zinc. These studies highlight the contributions of protein-protein interactions to metal speciation. Metal sensors and metallochaperones, along with metal transporters and metal-storage proteins, act in concert not only to supply the correct metals but also to withhold the wrong ones.

摘要

每种金属蛋白都必须以某种方式获取正确的金属。我们回顾了通过对ArsR-SmtB DNA结合、金属响应转录阻遏物和一种细菌铜伴侣蛋白的研究,所获得的关于细胞中金属特异性的见解。蓝细菌是已知对细胞质铜导入有酶需求的唯一细菌类群。本文综述了为蓝细菌质体蓝素和细胞色素氧化酶提供铜的伴侣蛋白和ATP酶,以及与钴和锌相关的ATP酶。这些研究突出了蛋白质-蛋白质相互作用对金属形态的贡献。金属传感器和金属伴侣蛋白,以及金属转运蛋白和金属储存蛋白,协同作用,不仅提供正确的金属,还能阻止错误的金属进入。

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