Weiss Celeste, Jebara Fady, Nisemblat Shahar, Azem Abdussalam
George S. Weiss Faculty of Life Sciences, Department of Biochemistry and Molecular Biology, Tel Aviv University Tel Aviv, Israel.
Front Mol Biosci. 2016 Dec 8;3:80. doi: 10.3389/fmolb.2016.00080. eCollection 2016.
The GroEL-GroES chaperonin system is probably one of the most studied chaperone systems at the level of the molecular mechanism. Since the first reports of a bacterial gene involved in phage morphogenesis in 1972, these proteins have stimulated intensive research for over 40 years. During this time, detailed structural and functional studies have yielded constantly evolving concepts of the chaperonin mechanism of action. Despite of almost three decades of research on this oligomeric protein, certain aspects of its function remain controversial. In this review, we highlight one central aspect of its function, namely, the active intermediates of its reaction cycle, and present how research to this day continues to change our understanding of chaperonin-mediated protein folding.
GroEL - GroES伴侣蛋白系统可能是在分子机制层面研究最为深入的伴侣蛋白系统之一。自1972年首次报道一个参与噬菌体形态发生的细菌基因以来，这些蛋白质已经激发了长达40多年的深入研究。在此期间，详细的结构和功能研究不断催生有关伴侣蛋白作用机制的新观念。尽管对这种寡聚蛋白进行了近三十年的研究，但其功能的某些方面仍存在争议。在本综述中，我们着重介绍其功能的一个核心方面，即其反应循环的活性中间体，并阐述时至今日的研究如何持续改变我们对伴侣蛋白介导的蛋白质折叠的理解。
