OsCPK12对OsCATA和OsCATC进行酸化,以调节H2O2平衡,并改善大米中氧化应激耐受性
Beifang Wang1, Pao Xue2, Yingxin Zhang2
1State Key Laboratory of Rice Biology and Breeding, China National Rice Research Institute, Hangzhou 311400, China; Northern Rice Research Center of Bao Qing, Shuangyashan 155600, China; Zhejiang Key Laboratory of Super Rice Research, China National Rice Research Institute, Hangzhou 311400, China.
Plant communications
|December 22, 2023
概括
赖子依赖蛋白激酶12 (OsCPK12) 通过酸化酶酶来调节抗氧化防御. 这种机制改善过氧化的稳态,并提高了大米植物的氧化应激耐受性.
科学领域:
- 植物分子生物学 植物分子生物学
- 植物生理学 植物生理学
- 生物化学 生化学
背景情况:
- 取决于的蛋白激酶 (CPK) 是关键的植物传感器,参与生长,发育和应激反应.
- 植物抗氧化剂防御系统调节中CPKs的确切作用,特别是有关过氧化 (H2O2) 恒温的作用,尚未完全理解.
- 之前的研究表明,大米中OSCPK12功能受损导致氧化应激,其特征是H2O2升高,酶 (CAT) 活性降低,产量降低.
研究的目的:
- 阐明OsCPK12在调解大米中氧化应激耐受性的特定作用.
- 调查OsCPK12影响抗氧化剂防御系统的分子机制,重点关注酶活性.
主要方法:
- 研究了OsCPK12.12对催化酶 (OsCATA和OsCATC) 的相互作用和酸化.
- 利用OsCATA和OsCATC的淘汰突变来评估它们在氧化应激中的作用.
- 采用模仿突变物 (OsCATAS11D和OsCATCS11D) 和OsCPK12过度表达线来评估H2O2水平和CAT活性.
- 进行了体内和体外测试,以测量催化酶活性.
主要成果:
- OsCPK12直接与OsCATA和OsCATC在Serine 11 (Ser11) 相互作用并酸化它们.
- 在OsCATA或OsCATC中的功能丧失突变导致H2O2积累增加和氧化应激表型.
- 过度表达的相仿性OsCATAS11D和OsCATCS11D降低了H2O2水平并增强了CAT活动.
- 过度表达OsCPK12的米植物表现出较高的CAT活性和对氧化应激的耐受性.
结论:
- OsCPK12通过调节酶活性,在米的氧化应激耐受性中发挥重要作用.
- OsCPK12在Ser11中对OsCATA和OsCATC的酸化是维持H2O2平衡的关键调节步骤.
- 这种OsCPK12介导的酸化途径对于调节抗氧化剂防御系统和赋予大米对氧化应激的耐受性至关重要.
相关概念视频
Regulation of Transpiration by Stomata
28.3K
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.
28.3K
Adaptations that Reduce Water Loss
25.6K
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.
25.6K
Responses to Salt Stress
13.1K
Salt stress—which can be triggered by high salt concentrations in a plant’s environment—can significantly affect plant growth and crop production by influencing photosynthesis and the absorption of water and nutrients.
13.1K
Peroxisomes
12.8K
Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
12.8K
The Unfolded Protein Response
4.6K
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...
4.6K
Regulation of the Unfolded Protein Response
2.4K
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...
2.4K


