Marchenko N Iu, Marchenkov V V, Kotova N V, Semisotnov G V, Bulankina N I, Kaliman P A
Karazin Kharkiv National University, Ukraine.
Ukr Biokhim Zh (1999). 2003 May-Jun;75(3):88-94.
The interaction of the molecular chaperonin GroEL with fluorescein-labeled lysozyme in the presence of high concentrations of thiol reagent--dithiothreitol (DTT) has been studied. In case of high concentrations of DTT lysozyme loses the native conformation due to the disruption of the intramolecular disulfide bonds stabilizing its structure and effectively aggregates. It has been shown that in the presence of high concentrations of DTT and two-fold molar excess of GroEL the lysozyme tightly interacts with GroEL that essentially decreases the efficiency of its aggregation. The addition of ADP to the complex of GroEL with nonnative lysozyme noticeably decreases the interaction of the chaperonin with nonnative protein target resulting in some increase of the efficiency of its aggregation. However, the addition of the co-chaperonin GroES together with ADP (i.e. the formation of the complex of GroEL with GroES) leads to drastic weakness of the interaction of GroEL with nonnative lysozyme and the efficiency of its aggregation becomes comparable with that in the absence of GroEL.
在高浓度硫醇试剂二硫苏糖醇（DTT）存在的情况下，对分子伴侣蛋白GroEL与荧光素标记的溶菌酶之间的相互作用进行了研究。在高浓度DTT的情况下，溶菌酶由于稳定其结构的分子内二硫键被破坏而失去天然构象，并有效聚集。研究表明，在高浓度DTT和两倍摩尔过量的GroEL存在下，溶菌酶与GroEL紧密相互作用，这基本上降低了其聚集效率。向GroEL与非天然溶菌酶的复合物中添加ADP会显著降低伴侣蛋白与非天然蛋白质靶标的相互作用，导致其聚集效率有所提高。然而，将共伴侣蛋白GroES与ADP一起添加（即形成GroEL与GroES的复合物）会导致GroEL与非天然溶菌酶的相互作用急剧减弱，其聚集效率变得与没有GroEL时相当。
