在 chaperonin 辅助折叠的过程中监测蛋白质构造
Shruti Sharma1, Kausik Chakraborty, Barbara K Müller
1Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Cell
|April 9, 2008
概括
细菌GroEL/GroES陪伴系统和上游DnaK/DnaJ (Hsp70) 协助蛋白质折叠. 这项研究揭示了GroEL/GroES如何展开,然后通过形状变化重新折叠蛋白质,防止错误折叠.
科学领域:
- 分子生物学分子生物学
- 生物化学 生物化学
- 蛋白质折叠 蛋白质的折叠
背景情况:
- 在细菌中,GroEL/GroES chaperonin 系统对于蛋白质折叠至关重要.
- 新合成的蛋白质在达到GroEL之前与上游的护卫体 (如DnaK/DnaJ (Hsp70)) 相互作用.
研究的目的:
- 使用单分子和集合FRET监测DnaK/DnaJ沿DnaK/DnaJ到GroEL/GroES陪伴子通路的模型基质的构造过渡.
- 阐明GroEL/GroES促进蛋白质折叠的机制.
主要方法:
- 单分子弗斯特共振能量转移 (smFRET) 技术
- 合唱团FRETET的组成部分.
- 监测模型基质蛋白质的构造变化.
主要成果:
- DnaK/DnaJ (Hsp70) 稳定了缓慢折叠,崩的蛋白质状态.
- GroEL诱导展开和局部扩张,随后是依赖ATP的调动和中度疏水细分的部分紧缩.
- GroES封装导致完整的紧缩和快速折叠,特别是在更疏水的区域.
结论:
- GroEL/GroES系统通过分段链释放和压缩,积极展开和重新折叠蛋白质.
- 这种机制可以防止错误折叠,特别是对于那些通过自发性疏水性崩而不能有效折叠的蛋白质.
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