Kawata Y, Hongo K, Nosaka K, Furutsu Y, Mizobata T, Nagai J
Department of Biotechnology, Faculty of Engineering, Tottori University, Japan.
FEBS Lett. 1995 Aug 7;369(2-3):283-6. doi: 10.1016/0014-5793(95)00768-5.
In order to understand the role of ATP hydrolysis of the chaperonin GroEL during protein folding, we have studied GroEL-GroES complex formation in the presence of ATP or ADP by using capillary electrophoresis and surface plasmon resonance. Capillary electrophoresis analysis showed that the GroEL 14-mer and GroES 7-mer formed a 1:1 complex in the presence of ATP. In the presence of ADP, both the association and dissociation rates of the complex were slower by about one order of magnitude than the rates in the presence of ATP at 25 degrees C. The implications of such a stable complex on the overall mechanism of chaperonin function are discussed.
为了了解伴侣蛋白GroEL的ATP水解在蛋白质折叠过程中的作用，我们利用毛细管电泳和表面等离子体共振研究了在ATP或ADP存在下GroEL-GroES复合物的形成。毛细管电泳分析表明，在ATP存在下，GroEL十四聚体和GroES七聚体形成了1:1的复合物。在ADP存在下，该复合物的缔合和解离速率在25℃时均比ATP存在时的速率慢约一个数量级。本文讨论了这种稳定复合物对伴侣蛋白功能整体机制的影响。
