揭示了在质体内膜外的蛋白质转位子
Shingo Kikuchi1, Jocelyn Bédard, Minako Hirano
1Laboratory of Regulation of Biological Reactions, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, Japan.
概括
包括Tic20和Ycf1在内的内膜蛋白转位子 (TIC) 综合体被净化,并被证明形成了前蛋白敏感通道,将其确定为一般的TIC转位子.
科学领域:
- 植物细胞生物学 植物细胞生物学
- 叶绿体生物生成 叶绿体生物生成
- 蛋白质的运输方式
背景情况:
- 叶绿体通过TOC和TIC转位孔进口蛋白质.
- 对TIC转位子的分子组成进行了辩论.
研究的目的:
- 为了识别TIC translocon.con. 的分子组成部分.
- 为了功能性地描述ICT复合体.
主要方法:
- 从阿拉比多普西斯中净化1兆达尔顿的TIC复合物.
- 复杂组件的软度分析.复杂组件的软度分析.
- 复合物的重构成平面脂质双层.
主要成果:
- 1兆的复合体包括Tic20,Ycf1和其他两个蛋白质.
- 这四个成分都与转位前蛋白有关.
- 净化的复合物形成了一个预蛋白门通道.
结论:
- 净化的复合体代表了一般的TIC转位连接.
- 这一发现解决了TIC转位子的分子身份.
相关概念视频
Protein Transport to the Inner Chloroplast Membrane
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Protein Transport to the Outer Chloroplast Membrane
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Protein Transport to the Stroma
Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein Transport to the Thylakoids
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
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...


