Department of Plant and Environmental Sciences, Gothenburg University, 40530 Gothenburg, Sweden.
Physiol Plant. 2012 May;145(1):235-44. doi: 10.1111/j.1399-3054.2011.01541.x. Epub 2011 Dec 15.
The ATP-dependent Clp protease is by far the most intricate protease in chloroplasts of vascular plants. Structurally, it is particularly complex with a proteolytic core complex containing 11 distinct subunits along with three potential chaperone partners. The Clp protease is also essential for chloroplast development and overall plant viability. Over the past decade, many of the important characteristics of this crucial protease have been revealed in the model plant species Arabidopsis thaliana. Despite this, challenges still remain in fully resolving certain key features, in particular, how the assembly of this multisubunit protease is regulated, the full range of native protein substrates and how they are targeted for degradation and how this complicated enzyme might have developed from simpler bacterial forms. This article focuses upon the recent advances in revealing the details underlying these important features. It also take the opportunity to speculate upon many of these findings in the hope of stimulating further investigation.
ATP 依赖的 Clp 蛋白酶是迄今为止在维管植物叶绿体中最复杂的蛋白酶。从结构上看，它特别复杂，具有一个包含 11 个不同亚基的蛋白水解核心复合物，以及三个潜在的伴侣蛋白。Clp 蛋白酶对于叶绿体的发育和植物整体的生存能力也是至关重要的。在过去的十年中，许多关于这种关键蛋白酶的重要特征已经在模式植物拟南芥中被揭示。尽管如此，在完全解析某些关键特征方面仍然存在挑战，特别是这种多亚基蛋白酶的组装是如何被调控的，以及完整的天然蛋白底物的范围，以及它们是如何被靶向进行降解的，以及这种复杂的酶是如何从更简单的细菌形式发展而来的。本文主要关注揭示这些重要特征背后的最新进展。它还借此机会对这些发现中的许多内容进行推测，希望能激发进一步的研究。
