在Saccharomyces cerevisiae中,Isa2p对于线粒体功能和抗压能力至关重要,因为它允许Rip1p亚单元组装成细胞染色体bc复合体
Luis A Sánchez-Briones1, Mauricio Gomez-Gallardo, Christian Cortes-Rojo
1Laboratorio de Biotecnología Microbiana, Instituto de Investigaciones Químico Biológicas, Universidad Michoacana de San Nicolás de Hidalgo, Morelia, Michoacán, México.
Journal of biosciences
|July 11, 2025
概括
铁硫集群生物发生子系统蛋白 Isa2p 对于酵母呼吸功能和氧化应激抵抗是至关重要的. ISA2中的突变破坏了铁硫蛋白的插入,影响了电子运输链超级复合体和乙醇应激耐受性.
科学领域:
- 细胞生物学 细胞生物学
- 生物化学 生物化学
- 线粒体功能的功能
背景情况:
- 在酵母中,铁硫生物生成晚效子系统 (Fe-S-IBG) 对于将 [4Fe-4S] 集群插入阿波蛋白至关重要.
- 它通过[Fe-S]蛋白质插入稳定呼吸系统超级复合体和电子运输链 (ETC) 功能的作用需要进一步研究.
研究的目的:
- 研究Isa2p和Grx5p在Fe-S-IBG子系统中的作用.
- 确定Isa2p是否对Rip1p插入,呼吸超复杂组合和氧化应激抵抗至关重要.
主要方法:
- 独立ISA2和GRX5突变在单体Saccharomyces cerevisiae中的比较分析.
- 评估Rip1p水平,超复杂组装,ETC功能和氧化/乙醇应激抵抗.
- 评估谷氨氧化和自由铁水平.
主要成果:
- ISA2Δ 和 GRX5Δ 突变体对乙醇压力的敏感性增加,这与高的谷氨氧化和自由铁有关.
- 突变的ISA2Δ显示减少了Rip1p表达,呼吸功能受损,以及缺陷的超级复合体形成.
- 与ISA2的补充恢复了ISA2Δ突变体中的这些缺陷.
结论:
- Isa2p对于维持适当的呼吸链功能和酵母菌中抗氧化应激能力至关重要.
- Isa2p的功能涉及稳定呼吸系统超级复合体,取决于Rip1p插入细胞染色体bc复合体.
- Fe-S-IBG子系统在细胞防御中发挥着关键作用,可以抵抗氧化和乙醇诱导的压力.
更多相关视频
相关概念视频
The Supercomplexes in the Crista Membrane
2.6K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.6K
Translocation of Proteins into the Mitochondria
3.6K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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,...
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,...
3.6K
Regulation of the Unfolded Protein Response
2.6K
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...
2.6K
The Inner Mitochondrial Membrane
3.7K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria. In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
3.7K
Mitochondrial Protein Sorting
4.4K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.4K
Protein Transport into the Inner Mitochondrial Membrane
4.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Transport of mitochondrial precursors across the TIM23 channel is driven by...
4.1K


