AraC protein: a love-hate relationship
AraC protein: a love-hate relationship
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DOI：
10.1002/bies.10237
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发表时间：
2003-03-01
期刊：
影响因子：
4
通讯作者：
Schleif, R
中科院分区：
文献类型：
--
作者：
Schleif, R
在大肠杆菌中，AraC蛋白正或负调节l -阿拉伯糖的摄取和分解代谢所需的tale蛋白的表达。这篇文章描述了如何在我的实验室工作在这个系统跨越三十多年来帮助我们理解积极的监管,发现DNA循环的特点在于远距离行为(一种机制来解释许多现象),最近,发现了树胶醛醣AraC从一个状态转移的机制,它更愿意绑定到两个DNA half-sites布置得井然有序,形成DNA循环状态,结合两个相邻half-sites和激活转录。这项工作需要学习如何分析、纯化和处理具有高度不合作生化特性的蛋白质。目前的工作主要集中在原子细节上理解阿拉伯糖反应机制，也针对蛋白质结构和功能的理解，以便能够将在AraC中看到的变构机制设计到其他蛋白质上。
In the bacterium Escherichia coh, the AraC protein positively and negatively regulates expression of tale proteins required for the uptake and catabolism of the sugar L-arabinose. This essay describes how work from my laboratory on this system spanning more than thirty years has aided our understanding of positive regulation, revealed DNA looping (a mechanism that explains many action-at-a-distance phenomena) and, more recently, has uncovered the mechanism by which arabinose shifts AraC from a state where it prefers to bind to two well-separated DNA half-sites and form a DNA loop to a state where it binds to two adjacent half-sites and activates transcription. This work required learning how to assay, purify, and work with a protein possessing highly uncooperative biochemical properties. Present work is focussed on understanding arabinose-responsive mechanism in atomic detail and is also directed towards understanding protein structure and function well enough to be able to engineer the allosteric mechanism seen in AraC onto other proteins.