在热冲击应力下,OsTrxm的功能变化从减少酶变成分子伴侣
Ho Byoung Chae1, Young Jun Jung2, Seol Ki Paeng1
1Division of Applied Life Sciences (BK21(+)), PMBBRC, and Plant Biological Rhythm Research Center, Gyeongsang National University, Jinju, 52828, South Korea.
Plant physiology and biochemistry : PPB
|September 30, 2023
概括
铁素 (Trxs) 对氧化还原平衡至关重要. 这项研究揭示了米Trx m型 (OsTrxm) 活性氨酸对结构变化至关重要,通过分子伴侣和二硫化还原酶功能赋予耐热性.
科学领域:
- 植物生物学 植物生物学
- 生物化学 生物化学
- 分子生物学分子生物学
背景情况:
- 铁素 (Trxs) 是必不可少的二硫化还原酶,调节所有生命形式的氧化还原平衡.
- 虽然已知米Trx m型 (OsTrxm) 在质体发育中的作用,但其生物化学和分子功能需要进一步阐明.
- 了解OsTrxm的功能对于植物应激反应机制至关重要.
研究的目的:
- 通过使用Arabidopsis thaliana来研究OsTrxm中活体囊素的体内作用.
- 描述OsTrxm及其突变形式 (OsTrxmC/S) 的生物化学和分子功能.
- 为了确定 OsTrxm 结构,功能和耐热性之间的关系.
主要方法:
- 在Arabidopsis thaliana中过度表达OsTrxm和OsTrxmC/S蛋白质.
- 细菌表达和分离纯化的OsTrxm和OsTrxmC/S蛋白质.
- 分析蛋白质结构 (LMW和HMW复合体) 和相关功能 (二硫化减少酶和分子陪伴剂).
主要成果:
- 过度表达osTrxm的植物表现出对热冲击的增强抵抗力.
- OsTrxmC/S,形成更高分子量 (HMW) 复合体,显示出比OsTrxm (较低分子量,LMW) 更大的耐热性.
- 对于OsTrxm和OsTrxmC/S,确定了LMW和HMW复合体,它们表现出明显的二硫化还原酶和分子伴侣活动.
结论:
- 在热应力下,OsTrxm中的活性囊对其结构性可塑性至关重要.
- OsTrxm作为二硫化还原酶 (主要在LMW形式) 和分子伴侣 (主要在HMW复合体中) 起作用.
- 这些双重功能对植物的耐热性做出了重大贡献,突出了OsTrxm的新角色.
相关概念视频
Other Stress Responses in Bacteria
30
Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
30
Bacterial Protein Maturation
33
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
33
Molecular Chaperones and Protein Folding
18.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.0K
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
Diversity of Archaea III
28
Crenarchaeota, a prominent phylum of Archaea, is remarkable for its ability to thrive in extreme environments characterized by high temperatures and acidity. These microorganisms inhabit sulfuric hot springs, volcanic systems, and submarine hydrothermal vents, where temperatures often exceed 100°C. The unique adaptations of Crenarchaeota not only allow survival under such extreme conditions but also provide insights into the mechanisms of life in primordial Earth-like...
28
Protein Modifications in the RER
5.2K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.2K


