Melegh B, Minami Y
MTA-POTE Genetic Research Group of Hungarian Academy of Sciences, Department of Genetics, University Medical School of Pécs, Hungary.
Acta Biol Hung. 1997;48(4):399-407.
For studying the possible interaction between the chaperonins and phosphofructokinase (PFK), bacterial chaperonins GroEL, GroES, and the PFK were co-purified from chaperonin over-expressing, heat treated E. coli strains. GroEL interacted with PFK in the presence of Mg2+, leading to a gradual decrease in the activity of the enzyme. This type of GroEL-PFK interaction was overcame by the GroES. On the effect of the addition of ATP to the GroEL-PFK complex, the decreased activity of the enzyme was recovered suggesting release of the GroEL-bound enzyme. Contrary to this, in a complete refolding system containing GroEL, GroES, ATP and Mg2+, activity of heat treated bacterial PFK gradually increased showing, that GroEL and GroES together play a role in the folding and/or assembly of PFK. Similar effect of refolding system was also observed on rabbit muscle PFK. The data show that PFK can interact with GroEL, which results in binding of the enzyme; by contrast, GroEL and GroES together has a folding effect leading ultimately to increase of the activity of the enzyme.
为了研究伴侣蛋白与磷酸果糖激酶（PFK）之间可能的相互作用，从过表达伴侣蛋白且经过热处理的大肠杆菌菌株中共同纯化出细菌伴侣蛋白GroEL、GroES和PFK。在Mg2+存在的情况下，GroEL与PFK相互作用，导致该酶的活性逐渐降低。这种GroEL-PFK相互作用类型可被GroES克服。在向GroEL-PFK复合物中添加ATP的影响下，酶活性的降低得以恢复，表明与GroEL结合的酶被释放。与此相反，在含有GroEL、GroES、ATP和Mg2+的完整重折叠系统中，热处理的细菌PFK活性逐渐增加，表明GroEL和GroES共同在PFK的折叠和/或组装中发挥作用。在兔肌肉PFK上也观察到了重折叠系统的类似效果。数据表明，PFK可与GroEL相互作用，这导致酶的结合；相比之下，GroEL和GroES共同具有折叠作用，最终导致酶活性增加。
