在膜载体的转位途径中识别残留物
1Department of Physiology, Johns Hopkins University Medical School, Baltimore, Maryland 21209.
Cell
|October 8, 1993
概括
氨酸残留物对于大肠杆菌的葡萄糖6酸盐输送体 (UhpT) 功能来说并不必不可少. 然而,C265对于运输至关重要,因为它直接位于基质通路上.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 膜运输 运输 膜运输
背景情况:
- UhpT是一种大肠杆菌的离子交换蛋白,可促进葡萄糖-6酸盐的运输.
- 之前的研究表明,氨酸残留物对于UhpT的运行并不重要.
研究的目的:
- 调查特定的氨酸残留物 (C143和C265) 在UhpT功能和基质运输中的作用.
- 为了确定C143和C265在大肠杆菌膜中的位置和可访问性.
主要方法:
- 用定向突变发生来评估囊的需求.
- 用p-chlomercuribenzosulfonate (PCMBS) 的反应来探测囊素的可访问性.
- 进行了基质结合试验,以评估葡萄糖6酸盐对PCMBS可访问性的影响.
主要成果:
- 氨酸残留物不需要用于UhpT的基本运输功能.
- C143位于膜的细胞质侧.
- C265可以从膜的两侧访问,其通过PCMBS的修改被葡萄糖6酸盐阻断.
结论:
- 虽然C265不是功能必不可少的,但在UhpT的传输机制中起着至关重要的作用.
- C265位于葡萄糖-6酸盐输送体的基质转位通路内.
相关概念视频
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
Translocation of Proteins into the Mitochondria
8.8K
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,...
8.8K
Protein Transport into the Inner Mitochondrial Membrane
3.5K
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...
3.5K
Cotranslational Protein Translocation
8.3K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
8.3K
Insertion of Single-pass Transmembrane Proteins in the RER
13.0K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
13.0K
Protein Translocation Machinery on the ER Membrane
5.5K
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...
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...
5.5K


