相关实验视频
Updated: Jul 28, 2025

07:43
Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
14.6K
叶子平衡通过在细胞质凝聚物中依赖于乌比奎的降解和封存来调节
Ulla Dolde1, Fernando Muzzopappa2, Charlotte Delesalle1
1Plant Science Research Laboratory (LRSV), UMR5546 CNRS/University of Toulouse/Toulouse-INP, 24 chemin de Borde Rouge, 31320 Auzeville Tolosane, France.
iScience
|June 1, 2023
概括
转录因子 LEAFY (LFY) 形成细胞质凝聚物,在那里它被UFO无处不在化以降解. 破坏这些凝聚物将LFY移动到核中,激活花发育基因.
科学领域:
- 植物分子生物学 植物分子生物学
- 细胞调节 细胞调节
- 转录因子的功能转录因子的功能
背景情况:
- 转录因子 LEAFY (LFY) 对于花的发育至关重要,并激活花的同源基因.
- "E3无处不在酶UFO与LFY合作激活其目标,但该机制尚未完全理解.
研究的目的:
- 阐明UFO和LFY相互作用以调节花基因激活的机制.
- 研究LFY在控制其功能中的亚细胞局部化和稳定性的作用.
主要方法:
- 生物分子凝聚物形成试验 (体外和体内)
- 同免疫沉以检测蛋白质相互作用.
- 立方体化试验测定
- 蛋白质酶抑制和过度表达研究.
- 对LFY的突变分析.
- 用1,6-hexanediol进行处理以扰乱凝结物.
- 对花朵中LFY基因表达 (AP3) 的分析.
主要成果:
- 在细胞质生物分子凝聚物中积聚LFY.
- 再组合LFY在体外形成类似的凝结物.
- 在这些凝结物中,UFO与LFY相互作用,并将其定位为依赖于全方位素的降解.
- 核LFY水平是缓冲对影响总LFY水平的干扰.
- 细胞质LFY凝聚物的破坏导致LFY转移到细胞核,并激活AP3基因.
结论:
- 核细胞质分离,凝析物形成和依赖于泛素的降解是控制核LFY水平和活动的关键调节机制.
- 细胞质LFY冷凝剂充当缓冲核LFY度的储.
- 调节LFY凝结和降解对于精确控制花发育至关重要.
相关概念视频
Regulated Protein Degradation
7.4K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.4K
Adaptations that Reduce Water Loss
25.8K
Though evaporation from plant leaves drives transpiration, it also results in loss of water. Because water is critical for photosynthetic reactions and other cellular processes, evolutionary pressures on plants in different environments have driven the acquisition of adaptations that reduce water loss.
25.8K
Regulation of Transpiration by Stomata
28.5K
During photosynthesis, plants acquire the necessary carbon dioxide and release the produced oxygen back into the atmosphere. Openings in the epidermis of plant leaves is the site of this exchange of gasses. A single opening is called a stoma—derived from the Greek word for “mouth.” Stomata open and close in response to a variety of environmental cues.
28.5K
The Proteasome
915
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
915
Export of Misfolded Proteins out of the ER
3.7K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.7K
Regulation of the Unfolded Protein Response
2.5K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.5K

