通过CCT/TRiC对双β螺旋蛋白Coronin 7 (Coro7) 的域特定折叠
DeHaven J McCrary1, Teri Naismith1, Silvia Jansen1
1Department of Cell Biology and Physiology, Washington University in St. Louis, Saint Louis, MO, 63110, United States.
含有无尾复杂多1 (CCT/TRiC) 的Chaperonin chaperone有助于折叠多域蛋白质. 这项研究确定了冠状素7作为一种新的CCT/TRiC基质,揭示了其与初始β-螺旋域的伴侣相互作用.
科学领域:
- 细胞生物学 细胞生物学
- 蛋白质折叠机制 蛋白质折叠机制
- 分子陪伴者分子陪伴者
背景情况:
- 含有无尾复合聚1 (CCT) 的Chaperonin,也被称为TCP-1环复合体 (TRiC),对细胞平衡至关重要.
- CCT/TRiC伴随着丰富的细胞骨蛋白质,如actin和tubulin,并且越来越多地被认为是其在折叠WD40蛋白质中的作用.
- 以前,CCT/TRiC基质仅限于具有单个β-螺旋域的WD40蛋白.
研究的目的:
- 为了识别CCT/TRiC伴侣复合物的新基质.
- 为了研究CCT/TRiC与联β-螺旋蛋白的相互作用.
- 确定与CCT/TRiC相互作用的冠状素7的特定域.
主要方法:
- 生物素近距离结合试验.
- 质谱学分析的分析.
- 共同免疫沉实验的实验
- 暂时取消CCT/TRiC的使用.
- 对截断和特定域的冠状素7蛋白质的分析.
主要成果:
- 冠状素7 (Coro7),一个双β螺旋蛋白,被确定为CCT/TRiC的新型相互作用体.
- 暂时的CCT/TRiC淘汰显著降低了Coro7的表达,表明Coro7是CCT/TRiC基质.
- CCT/TRiC与Coro7的第一个β-螺旋域相互作用,而不是第二个.
结论:
- CCT/TRiC作为多β螺旋域蛋白质的伴侣,超越单域基板.
- 与第一个β-螺旋域的相互作用可能会启动后续域的折叠过程.
- 这一发现扩大了对CCT/TRiC的基质特异性及其在蛋白质折叠途径中的作用的理解.
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