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Protein conformational changes and molecular chaperone

蛋白质构象变化和分子伴侣

基本信息

批准号：
14037241
负责人：
KAWATA Yasushi
金额：
$ 72.45万
依托单位：
Tottori University
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research on Priority Areas
财政年份：
2002
资助国家：
日本
起止时间：
2002 至 2006
项目状态：
已结题

项目摘要

In order to understand how protein tertiary structure that is responsible for biofunction occurs and how molecular chaperones are involved in the event, we studied stabilities and conformational changes of various proteins, and clarified molecular mechanism of protein amyloid fibril formation. Furthermore, we studied functional mechanism of molecular chaperone, especially, chaperonins in detail, and obtained following results.1. Study on chaperonin mechanism: We have studied in detail structure and function relationship of group I chaperonin GroEL from E. coli and group II chaperonins from hyper-thermostable strains, from protein science and biophysical points of view. We have found that domain movements of GroEL are very important for the function and that cobalt and manganese ions are novel factors for nucleotide hydrolysis activity and substrate refolding function of group II chaperonin.2. Study on mechanism of protein amyloid fibril formation: We have found that oligomeric protein … More GroES, that is a non-related protein to disease, formed typical amyloid fibrils under unfolded conditions, and elucidated the fibril formation mechanism in terms of molecular compactness. Furthermore, we studied fibril formation mechanism of α-synuclein, that is a causative protein of Parkinson's disease, and proved that the amyloid fibril formation of α-synuclein is accelerated markedly in the presence of preformed seeds of other different protein's fibrils.3. Study on structure and stability of oligomeric protein: We have determined the X-ray crystal structure of thermostable aspartase enzyme, and elucidated the mechanism of thermostability and active site structure of the enzyme comprising from 4 identical subunits. On the other hand, we studied solution structure and molecular unfolding mechanism of E. coli co-chaperonin GroES heptamer at high protein concentrations by using small angle X-ray scattering. Furthermore, we clarified that the subunit interaction is quite important for the total structural stability. Less

为了了解蛋白质三级结构是如何发生的，以及分子伴侣是如何参与的，我们研究了各种蛋白质的稳定性和构象变化，并阐明了蛋白质淀粉样纤维形成的分子机制。在此基础上，我们对分子伴侣，特别是伴侣蛋白的作用机理进行了详细的研究，并取得了以下成果.分子伴侣作用机制的研究：我们详细研究了大肠杆菌Ⅰ型分子伴侣GroEL的结构和功能关系。从蛋白质科学和生物物理学的角度来看，我们发现GroEL的结构域移动对于其功能非常重要，钴和锰离子是II型伴侣蛋白的核苷酸水解活性和底物重折叠功能的新因子.蛋白质淀粉样纤维形成机制的研究：我们发现寡聚蛋白 ...更多信息 GroES是一种与疾病无关的蛋白质，在未折叠条件下形成典型的淀粉样纤维，并从分子紧密性方面阐明了纤维形成机制。此外，我们还研究了帕金森病的致病蛋白α-突触核蛋白的纤维形成机制，证明了在其他不同蛋白纤维的预形成种子存在下，α-突触核蛋白的淀粉样纤维形成显著加快.寡聚体蛋白的结构和稳定性研究：测定了耐热性内切酶的X-射线晶体结构，阐明了该酶由4个相同的亚基组成的热稳定性机制和活性中心结构。另一方面，我们研究了E.大肠杆菌共伴侣蛋白GroES七聚体在高蛋白浓度通过使用小角X射线散射。此外，我们阐明了亚基相互作用是相当重要的整体结构的稳定性。少

项目成果

期刊论文数量（75）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

河田康志: "タンパク質化学, 第4巻, 酵素4.4リアーゼ[I], トリプトファナーゼ"廣川書店. 150-156 (2002)

川田靖：“蛋白质化学，第 4 卷，酶 4.4 裂解酶 [I]，色氨酸酶”广川书店 150-156（2002 年）。

DOI：
发表时间：
期刊：
影响因子：
0
作者：
通讯作者：

Hsp60 is Required for Blastema Formation and Maintenance during Regeneration

Hsp60 是再生过程中胚基形成和维持所必需的

DOI：
发表时间：
2005
期刊：
Proc. Natl. Acad. Sci. USA 102・41
影响因子：
0
作者：
Shinji Makino;Geoffrey G.Whitehead;Ching-Ling Lien;Akane Kono;Yasushi Kawata;Mark T.Keating
通讯作者：
Mark T.Keating

X.Fu et al.: "Induction of AApoAII Amyloidosis by Various Heterogeneous Amyloid Fibrils"FEBS Letters. (印刷中). (2004)

X.Fu 等人：“各种异质淀粉样原纤维诱导 AApoAII 淀粉样变性”FEBS Letters（2004 年出版）。