在其活性状态下,SecA蛋白暴露于大肠杆菌内膜的周等离子体表面
Y J Kim1, T Rajapandi, D Oliver
1Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, Connecticut 06459.
Cell
|September 9, 1994
概括
整体膜SecA蛋白是细菌蛋白质分泌中的活性形式. 在secDsecF的位置产品调节SecASecA.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 细菌蛋白质分泌 细菌蛋白质分泌
背景情况:
- SecA蛋白是一种关键的ATPase电机,驱动蛋白质在细菌内膜上的转移.
- 精确的局部化和SecA与膜相互作用的调节仍然是理解蛋白质分泌的关键问题.
研究的目的:
- 为了研究secD secF locus在调节SeCA定位和活动中的作用.
- 为了确定SeCA的催化活性形式及其在内膜内的可访问性.
主要方法:
- 在大肠杆菌中表达secD secF位点的表达.
- 使用膜囊泡的生物化学测定 (蛋白酶和生物化可访问性研究).
- 对SecA蛋白的局部化和转位活动的分析.
主要成果:
- 主要发现SecA蛋白质是整体膜形式,表现出正常的蛋白质转位活性.
- SecA可以进入内膜的周等离子体表面.
- secD secF 位点的产物被证明可以调节 SecA 与内膜的关联.
结论:
- 整体膜SecA是该酶的催化活性形式.
- secD secF 位产物调节SeCA 插入/退出内部膜,调节蛋白质导通通道组合.
- 提出了一个模型,其中SecA插入内膜,加上SecY/E/G,形成活跃的分泌通道.
相关概念视频
Role of ER in the Secretory Pathway
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
ER Retrieval Pathway
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Directing Proteins to the Rough Endoplasmic Reticulum
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Cotranslational Protein Translocation
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...
Insertion of Single-pass Transmembrane Proteins in the RER
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...
Post-translational Translocation of Proteins to the RER
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...


