相关实验视频
Updated: Jul 20, 2026

09:42
Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
Published on: June 19, 2012
SecB的抗折叠活性促进了大肠杆菌马尔托结合蛋白的出口
D N Collier1, V A Bankaitis, J B Weiss
1Department of Microbiology and Immunology, School of Medicine, University of North Carolina, Chapel Hill 27514.
Cell
|April 22, 1988
概括
大肠杆菌 secB 基因产物SecB对于蛋白质出口至关重要. 它与前体麦芽糖结合蛋白 (MBP) 结合,防止过早折叠,并确保有效的细胞外运输.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 蛋白质的运输方式
背景情况:
- 大肠杆菌中的secB基因对于蛋白质穿过内膜的输出至关重要.
- 马尔托结合蛋白 (MBP) 是对蛋白质出口途径进行了充分研究的模型系统.
研究的目的:
- 阐明SecB蛋白质促进大肠杆菌中马尔托结合蛋白 (MBP) 出口的机制.
- 研究SecB和前体MBP之间的相互作用及其在防止错误折叠方面的作用.
主要方法:
- 使用遗传和生化方法研究SecB和前体MBP之间的相互作用.
- 分析SecB可用性对MBP出口和折叠的影响.
- 使用体外合成和折叠试验来评估SecB的抗折叠活性.
主要成果:
- SecB与前体MBP的成熟区域直接相互作用.
- SecB可以防止新合成的MBP过早折叠成不适合出口的形状.
- SecB的可用性是MBP出口的限制因素,出口缺陷的MBP物种的干扰证明了这一点.
- SecB的缺席加快了MBP的折叠,而它的存在则延迟了它.
结论:
- 通过抑制其折叠,SecB作为一个陪伴者,通过抑制其折叠,保持前体MBP在出口能力的状态.
- 这种抗折叠活性对于E. coli中有效的SecB介导蛋白质出口至关重要.
相关概念视频
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
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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...
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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...
Export of Misfolded Proteins out of the ER
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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.
Bacterial Translocation and Protein Secretion
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...

