Makino Y, Taguchi H, Yoshida M
Research Laboratory of Resources Utilization, R-1, Tokyo Institute of Technology, Yokohama, Japan.
FEBS Lett. 1993 Dec 27;336(2):363-7. doi: 10.1016/0014-5793(93)80838-l.
Similar to chaperonins from other sources, intact chaperonin from Escherichia coli (GroEL) exists as a tetradecamer, and the ability to promote folding of other proteins has been considered to be dependent on this oligomeric structure. However, the peptide fragments of GroEL of molecular size 34-50 kDa, which are produced by limited proteolysis of monomeric GroEL and are unable to assemble into an oligomer, retain the ability to promote folding of rhodanese even though the yield of productive folding is lower than the intact GroEL/GroES/ATP system. This promotion by truncated GroEL obeys rapid kinetics and does not require GroES and ATP.
与其他来源的伴侣蛋白类似，来自大肠杆菌的完整伴侣蛋白（GroEL）以十四聚体形式存在，促进其他蛋白质折叠的能力被认为取决于这种寡聚结构。然而，分子大小为34 - 50 kDa的GroEL肽片段，由单体GroEL的有限蛋白酶解产生，无法组装成寡聚体，尽管有效折叠的产率低于完整的GroEL/GroES/ATP系统，但仍保留促进硫氰酸酶折叠的能力。这种截短的GroEL的促进作用遵循快速动力学，并且不需要GroES和ATP。
