汉塞努拉多态型线粒体载体家族蛋白Mir1在过氧体和线粒体的双重局部化
Marc Pilegaard Pedersen1, Justina C Wolters2, Rinse de Boer1
1Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands.
概括
酵母中的线粒体酸盐载体Mir1具有对线粒体和过氧体的双重定位. 特定的过氧素 (Pex3,Pex19) 和全长的Mir1对于其过氧体向至关重要.
科学领域:
- 细胞生物学 细胞生物学
- 机体生物学 机体生物学
- 贩卖蛋白质 贩卖蛋白质 是一个问题.
背景情况:
- 过氧体是具有不同代谢作用的重要器官.
- 有效的功能需要分子穿过氧体膜的运输.
- 氧体载体的鉴定仍然是一个活跃的研究领域.
研究的目的:
- 通过质谱学识别新的多氧体膜蛋白.
- 为了研究线粒体酸盐载体Mir1.1.的双重定位.
- 阐明控制Mir1对氧体进行分类的分子机制.
主要方法:
- 从Hansenula polymorpha中净化过氧体膜分量的蛋白质组学分析,使用非向的无标签量化质谱学.
- 基于光显微镜的蛋白质局部化研究在野生类型和突变酵母菌株.
- 对切断的Mir1变体进行分析,以确定功能排序域.
主要成果:
- 质谱测量确定了已知的过氧体蛋白和意想不到的线粒体载体,包括Mir1.1.
- Mir1对线粒体和过氧体都表现出双重定位.
- 佩克斯3和佩克斯19对于Mir1的氧体向是必不可少的,而只有一个特定的域 (跨膜域3-6),在截断的版本中显示了氧体定位.
- 对于过氧体局部化,需要全长的Mir1,这表明蛋白质内有多个线粒体排序信号.
结论:
- 线粒体酸盐载体Mir1是H. polymorpha.中的双局部蛋白质.
- Mir1的过氧体向取决于过氧素Pex3和Pex19.
- 全长的Mir1,而不仅仅是特定的域,对于过氧体排序是必要的,表明复杂的调节机制.
相关概念视频
Mitochondrial Protein Sorting
4.3K
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...
4.3K
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
Protein Import into the Peroxisomes
3.5K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
3.5K
Protein Transport into the Inner Mitochondrial Membrane
3.7K
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...
3.7K
Mitochondrial Precursor Proteins
2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
Most of the mitochondrial...
2.6K
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


