受到ERF28和NOR调节的ERF100控制了点酸酶7,调节无花果 (Ficus carica L.) 果软化剂
Zhiyi Fan1, Yuan Wang1, Yanlei Zhai1
1College of Horticulture, China Agricultural University, Beijing, China.
Plant biotechnology journal
|April 10, 2025
概括
无花果软化是由一个新的FcERF100转录因子复合体调节的. 这种复合体通过调节果实成熟期间的乳酸酶基因表达来控制细胞壁的修饰.
科学领域:
- 植物生物学 植物生物学
- 分子生物学分子生物学
- 生物化学 生化学
背景情况:
- 果实成熟涉及复杂的纹理变化,主要是由细胞壁的修改驱动的.
- 调节这些纹理变化的精确分子机制,特别是水果软化,仍然不完全理解.
研究的目的:
- 阐明无花果在成熟过程中的纹理变化背后的调节机制.
- 确定关键的转录因子及其与控制水果软化和细胞壁修饰有关的相互作用.
主要方法:
- 酵母一杂交 (Y1H) 和酵母两杂交 (Y2H) 对蛋白质-蛋白质和蛋白质-DNA相互作用的测定.
- 染色体免疫沉-qPCR (ChIP-qPCR) 和电泳运动转移试验 (EMSA) 用于直接促进体结合的验证.
- 双露西法酶记者测定用于评估转录活性.
- 生成稳定的转基因无花果系和基因沉默实验.
- 乙烯处理用于研究基因表达反应.
主要成果:
- 转录因子FcERF100直接抑制乳酸酸酶基因FcPL7,延迟无花果软化.
- FcERF28在上游作用,激活FcERF100,形成一个FcERF28-FcERF100级联,调节FcPL7.7.
- NAC转录因子FcNOR与FcERF100相互作用,减弱其对FcPL7的抑制,并抑制FcERF100的转录.
- 乙烯处理不同调节这些关键转录因子和FcPL7.7的表达.
结论:
- 一个新的以FcERF100为中心的调控复合体,涉及FcERF28和FcNOR,控制无花果软化.
- 这种复合物调节FcPL7的表达,平衡细胞壁的修饰,以促进早期的水果生长和晚期的成熟.
- 这些发现为控制水果发育和成熟的复杂转录网络提供了新的见解.
相关概念视频
01:29Protein Folding Quality Check in the RER
3.6K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.6K
01:58Fruit Development, Structure, and Function
21.9K
Fruits form from a mature flower ovary. As seeds develop from the ovules contained within, the ovary wall undergoes a series of complex changes to form fruit. In some fruits, such as soybeans, the ovary wall dries; in other fruits, such as grapes, it remains fleshy. In some cases, organs other than the ovary contribute to fruit formation; such fruits are called accessory fruits.
21.9K
01:31Regulation of the Unfolded Protein Response
2.3K
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...
2.3K
01:37The Unfolded Protein Response
4.3K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
4.3K
00:46Feedback Inhibition
53.4K
Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
53.4K
01:45Regulation of Nuclear Protein Sorting
2.3K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.3K