中文摘要：

Ydj1p是酵母细胞质中一种主要的I型Hsp40分子伴侣,Ydj1p锌指结构在传递底物给Hsp70时发挥重要的作用,锌指结构域的两个锌离子结合位点区域（ZBDⅠ和ZBDⅡ）与半胱氨酸形成配位键对底物传递中维持结构稳定非常重要。本研究通过分子动力学手段对Ydj1p与各锌指结构突变体进行了模拟,分析ZBDⅠ突变体关键残基C143S、C201S,ZBDⅡ突变体关键残基C162S、C185S的突变影响Hsp40与Hsp70的底物传递。分析结果表明,当锌指部位的氨基酸发生突变,不仅能影响Ydj1p的结构稳定性,也能影响底物的传递,并且锌指结构Ⅰ突变体和锌指结构Ⅱ突变体之间也具有明显差异。通过结合能量的分析以及构象变化比对,揭示了Ydj1p以及各锌指结构突变体底物结合能力的强弱,这与生化实验研究了Ydj1p锌指结构与Hsp70合作,帮助多肽传递的功能是至关重要的结果较为相近。

英文摘要：

Ydj1p is a major kind of I type Hsp40 molecular chaperone in yeast cytoplasm. Zinc finger structure plays a significant role in transmitting substrates to Hsp70. The two zinc binding sites region （ZBD I and ZBD II） in the zinc finger domain can form a coordination bond with cysteine, which is important for maintaining structural stability during the substrate transfer process. In this paper, Ydj l p and the various zinc structural mutants are studied by using the method of molecular dynamic simulation. How the mutations that take place in ZBD I mutant key residues C143S, C201S and ZBD II mutant key residues C162s, C185S affect the substrate transfer between Hsp40 and HspT0 are also analyzed. The results show that mutations in the amino acids in zinc finger sites not only affect the structural stability of Ydjlp, but also affect the substrate transport. Moreover, there are also significant differences between zinc finger type I mutants and zinc finger structure II mutants. It reveals how about the combining capacities of Ydj lp with the various zinc finger structure mutant substrates through the analysis of binding energy and the contrast of conformation changes are. The simulated result is similar to the results of the biochemistry experiments that the cooperation of Ydjlp zinc finger structure and Hsp70 is crucial to help pcptide transfer function.