导入载体蛋白质进入线粒体内膜,由Tim22介导
C Sirrenberg1, M F Bauer, B Guiard
1Institut für Physiologische Chemie der Universität München, Germany.
Nature
|December 12, 1996
概括
蒂姆22是一种新型蛋白质进口成分,对线粒体ADP/ATP载体 (AAC) 家族至关重要,其功能独立于酵母中的蒂姆23-蒂姆17复合体.
科学领域:
- 线粒体生物学 线粒体生物学
- 蛋白质进口机械 机械
背景情况:
- 线粒体蛋白质的进口对细胞功能至关重要.
- 内膜转位酶 (TIM) 机制有助于蛋白质转位.
- Tim23,Tim17,Tim44,Hsp70和Mgel是已知的参与矩阵蛋白质进口的组成部分.
研究的目的:
- 为了描述新发现的Tim22蛋白的功能.
- 确定Tim22在进口特定线粒体蛋白质中的作用.
主要方法:
- 研究了线粒体ADP/ATP载体 (AAC) 蛋白质的进口途径.
- 分析了Tim22与其他TIM组件的关联.
- 研究了AAC进口对Tim23的依赖,反之亦然.
主要成果:
- 蒂姆22对线粒体ADP/ATP载体 (AAC) 蛋白家族的进口至关重要.
- 在没有矩阵准信号的情况下合成AAC蛋白.
- 蒂姆22形成了一个独特的高分子质量组件,与蒂姆23-蒂姆17复合体分开.
结论:
- 蒂姆22代表了线粒体蛋白质进口机械的新型组件.
- 由Tim22介导的进口途径独立于Tim23-Tim17复合体.
- 这项研究阐明了像AAC.这样的内膜蛋白的独特进口路线.
相关概念视频
The ADP/ATP Carrier Protein
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
Mitochondrial Protein Sorting
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...
Mitochondrial Precursor Proteins
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 precursors...
Most of the mitochondrial precursors...
Translocation of Proteins into the Mitochondria
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,...
Energy to Drive Translocation
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
Protein Transport into the Inner Mitochondrial Membrane
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...


