酵母V-ATPase与TLDc蛋白Rtc5pp的相互作用
Md Murad Khan1, Roshanak Ebrahimi1, Rebecca A Oot1
1Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
bioRxiv : the preprint server for biology
|June 6, 2025
概括
Rtc5p有助于从其部分组装真空H+-ATPase (V-ATPase) 酶. 结构研究揭示了它的机制,表明存在多个V-ATPase组装路径.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 真空H+-ATPase (V-ATPase) 通过可逆分解到V1和Vo亚复合体来调节细胞过程.
- 了解V-ATPase组装的分子机制至关重要,但仍然不太了解.
- 已知oxr1p对于体内V-ATPase分解至关重要.
研究的目的:
- 阐明TLDc域蛋白质Rtc5p在V-ATPase可逆组合中的作用.
- 研究Rtc5p促进V-ATPase组装的分子机制.
主要方法:
- 在试验室组装测试中使用纯化的V1和Vo子复合体.
- 电子显微镜 (CryoEM) 用于确定Rtc5p-V-ATPase相互作用的结构细节.
- 在酵母中Rtc5p功能的表型分析.
主要成果:
- 在体外,Rtc5p促进了从纯化的V1和Vo亚复合体中组装功能全体V-ATPase.
- 低温EM结构显示,Rtc5p结合V1-B子单元并将α螺旋插入到催化六合体中,可能打开第二个催化部位.
- 与Oxr1p不同的是,Rtc5p在体内葡萄糖驱动的V-ATPase组合中并不必不可少.
结论:
- Rtc5p作为V-ATPase的组装因子,与Oxr1p的分解作用不同.
- 结构数据提供了关于Rtc5p介导的V-ATPase组装机制的见解.
- 这些发现表明,在体内存在多种,可能是并行的,V-ATPase组合和调节的途径.
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