相关实验视频
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Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
从酵母Hsp110 Sse1的晶体结构中了解Hsp70伴侣活性
Qinglian Liu1, Wayne A Hendrickson
1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Cell
|October 10, 2007
概括
热冲击蛋白110s (Hsp110s) 通过结构分析被揭示为Hsp70的近亲. 这一发现澄清了Hsp70超级家族内的进化联系和性机制.
科学领域:
- 分子生物学分子生物学
- 结构生物学 结构生物学
- 生物化学 生物化学
背景情况:
- 热冲击蛋白 (HSP) 对蛋白质平衡至关重要.
- Hsp70的陪伴者得到了很好的研究,而Hsp110被认为是遥远的亲戚.
- 了解Hsp110的结构和功能是Hsp70超级家族演变的关键.
研究的目的:
- 确定Hsp110s和Hsp70s之间的结构关系.
- 阐明控制Hsp70功能的全性机制.
- 为了研究Hsp110s.的进化起源.
主要方法:
- 用X射线晶体学确定Sse1 (一种Hsp110) 的2.4A分辨率结构与ATP.
- 对Hsp110和Hsp70域进行比较结构分析.
- 在Sse1和Hsp70同类中对64种突变变异的功能分析.
主要成果:
- Sse1的结构 (ATP) 显示Hsp110s是Hsp70的近亲.
- 在Sse1域之间广泛和保守的接口反映了Hsp70s.
- Sse1 ((ATP) 和Hsp70域之间的形状差异表明存在进化联系.
结论:
- Hsp110s是Hsp70s的进化保存亲属,可能代表一个祖先的Hsp70 (ATP) 状态.
- 这项研究提供了原子层面的洞察力,了解Hsp70s.内部的全沟通.
- Hsp110s作为核酸交换因子具有明显的功能,对酵母活力至关重要.
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