线粒体核糖体生物发生和氧化还原感应
Michele Brischigliaro1, Ana Sierra-Magro1, Ahram Ahn2
1Department of Neurology, University of Miami Miller School of Medicine, FL, USA.
FEBS open bio
|June 7, 2024
概括
线粒体生物生成涉及线粒体RNA和核蛋白,由组装因子指导. 最近的研究突出显示铁硫集群和氧化回归敏感的囊在调节线粒体翻译.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 线粒体蛋白质合成中,线粒体蛋白质的生物发生是至关重要的.
- 它涉及线粒体RNA和核编码蛋白质,由组装因子协调.
研究的目的:
- 概述目前对哺乳动物线粒体生物发生的理解.
- 突出最近关于铁硫集群和氧化还原敏感氨酸的发现.
主要方法:
- 生物化学研究是生物化学研究.
- 哺乳动物线粒体的冷电子显微镜 (cryo-EM)
主要成果:
- 铁硫集群被确定为结构部件和组装因素.
- 在线核糖体蛋白和组装因子中发现的对氧化素敏感的囊蛋白.
结论:
- 线粒体组装是复杂的,涉及协调的RNA处理和蛋白质结合.
- 铁硫集群和氧化还原敏感的氨酸可以作为氧化还原传感器,在压力下调节线粒体转化.
相关概念视频
Translocation of Proteins into the Mitochondria
3.1K
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,...
3.1K
Mitochondrial Membranes
10.0K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
10.0K
The Supercomplexes in the Crista Membrane
2.5K
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...
2.5K
Porin Insertion in the Outer Mitochondrial Membrane
3.0K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
3.0K
Mitochondria
12.2K
Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
12.2K
Structure of Porins
3.0K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K


