由 SelO 催化的 NAD+ 水解是线粒体平衡的必要条件
Xiaofan Jia1, Teng Zhang2, Chenxi Yang2
1Department of Pharmacology, Tianjin Key Laboratory of Inflammatory Biology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, State Key Laboratory of Experimental Hematology, School of Basic Medical Sciences, Tianjin Cancer Institute and Hospital, Tianjin Medical University Cancer Institute and Hospital, Tianjin Medical University, Tianjin, China; The Sichuan Provincial Key Laboratory for Genetic Diseases, Institute for Laboratory Medicine, Sichuan Provincial People's Hospital, School of Medicine, University of Electronic Science and Technology of China, Chengdu, China.
科学家们发现了一种新的线粒体反应,其中SELENOO (SelO) 降解尼古丁胺氨酸二核酸 (NAD+),影响脂质利用和细胞呼吸. 这一发现揭示了 prokaryotes 和 eukaryotes 中保存的 NAD+ 调节机制.
科学领域:
- 生物化学 生物化学
- 细胞生物学 细胞生物学
- 代谢调节 代谢调节 代谢调节
背景情况:
- 尼古丁胺胺氨基二核酸 (NAD+) 对于细胞过程至关重要.
- 线粒体内NAD+降解的机制尚未完全理解.
研究的目的:
- 阐明线粒体NAD+调节的新途径.
- 在线粒体矩阵中识别参与NAD+水解的蛋白质.
主要方法:
- 在NAD+结合蛋白的in silico选.
- 生物化学测试以表征酶活性.
- 分析与代谢酶的蛋白质-蛋白质相互作用.
主要成果:
- 发现的SELENOO (SelO) 通过利用Mn2+将NAD+解为NMN和AMP.
- 催化过程依赖于Selo的C端单半氨酸残留物.
- 塞洛与脂肪酸氧化酶 (FAO) 相关,影响脂质代谢.
- 反应在哺乳动物和细菌中保存,并对矩阵pH反应.
结论:
- 确定了一种新的,保守的线粒体途径,用于通过SELO降解NAD+.
- 这种途径在脂质利用和代谢平衡中起着重要作用.
- 这些发现提供了对空间时空NAD+调节及其跨物种生理重要性的见解.
更多相关视频
05:27Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
Published on: July 20, 2022
06:53Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase COX/SDH Double-labeling Histochemistry
Published on: November 23, 2011
相关概念视频
Electron Transport Chain: Complex III and IV
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Mitochondrial Membranes
The Supercomplexes in the Crista Membrane
Role of Reduced Coenzymes NADH and FADH₂
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
