Semenyuk P I, Orlov V N, Kurochkina L P
Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, Moscow, 119234, Russia.
Biochemistry (Mosc). 2015 Feb;80(2):172-9. doi: 10.1134/S0006297915020042.
Investigation of the chaperonin encoded by gene 146 of bacteriophage EL Pseudomonas aeruginosa that we characterized earlier has been continued. To reveal the mechanism of its functioning, new recombinant substrate proteins, fragments of gene product (gp) 183 containing the lysozyme domain were prepared. Their interaction with gp146 was studied. The influence of the phage chaperonin on the thermal aggregation of one of these gp183 fragments and endolysin (gp188) was investigated in both the presence and the absence of ATP by dynamic light scattering. In the absence of ATP, the phage chaperonin forms stable complexes with substrate proteins, thereby protecting them against thermal aggregation. Experimental data obtained for different substrate proteins are analyzed.
我们之前鉴定过的噬菌体EL铜绿假单胞菌基因146编码的伴侣蛋白的研究仍在继续。为了揭示其作用机制，制备了新的重组底物蛋白，即含有溶菌酶结构域的基因产物（gp）183片段。研究了它们与gp146的相互作用。通过动态光散射研究了噬菌体伴侣蛋白在有ATP和无ATP情况下对这些gp183片段之一和内溶素（gp188）热聚集的影响。在无ATP的情况下，噬菌体伴侣蛋白与底物蛋白形成稳定的复合物，从而保护它们免于热聚集。分析了针对不同底物蛋白获得的实验数据。
