Kawata Y, Nosaka K, Hongo K, Mizobata T, Nagai J
Department of Biotechnology, Faculty of Engineering, Tottori University, Japan.
FEBS Lett. 1994 May 30;345(2-3):229-32. doi: 10.1016/0014-5793(94)00456-0.
In the presence of ADP, the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins, but also prevented their irreversible heat inactivation in vitro. Without nucleotides the refolding reactions were arrested by GroEL. Addition of GroES and ADP to the reaction mixture initiated the refolding reactions and the enzyme activities were regained efficiently. The presence of GroE (GroEL and GroES) and ADP also protected against heat inactivation of native enzymes at various temperatures. These findings suggest that in the presence of GroES, nucleotide binding is an important event in the mechanism of GroEL-facilitated protein folding.
在存在二磷酸腺苷（ADP）的情况下，来自大肠杆菌的分子伴侣GroEL和GroES不仅促进了各种蛋白质的重折叠，还在体外防止了它们的不可逆热失活。没有核苷酸时，GroEL会阻止重折叠反应。向反应混合物中添加GroES和ADP会启动重折叠反应，并且酶活性能够有效地恢复。GroE（GroEL和GroES）和ADP的存在还能在不同温度下保护天然酶免受热失活。这些发现表明，在存在GroES的情况下，核苷酸结合是GroEL促进蛋白质折叠机制中的一个重要事件。
