酵母Sec蛋白质的组合参与了转移到内 плазма网膜中的转移,形成一个与膜结合的多子单元复合体
R J Deshaies1, S L Sanders, D A Feldheim
1Division of Biochemistry and Molecular Biology, University of California Berkeley 94720.
Nature
|February 28, 1991
概括
这项研究确定了一种蛋白质复合体,该复合体对于分泌蛋白质转移到内质网膜 (ER) 至关重要. 这些SEC61,SEC62和SEC63基因编码了这一重要的ER膜复合体的组成部分.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 分泌蛋白转移到内 плазма网膜 (ER) 是一个基本的细胞过程.
- 据信,这种过程是由不可分割的膜蛋白促进的.
- 之前的遗传研究已经确定了参与该途径的关键Saccharomyces cerevisiae基因 (SEC61,SEC62,SEC63).
研究的目的:
- 研究分泌蛋白转移到ER的分子机制.
- 描述由SEC61,SEC62和SEC63编码的蛋白质及其相互作用.
- 确认这些基因在促进蛋白质进口到ER流体中的作用.
主要方法:
- 在Saccharomyces cerevisiae中进行遗传选择,以识别关键基因.
- 用DNA测序来预测蛋白质结构.
- 对SEC62蛋白 (Sec62) 的生物化学表征.
- 蛋白质复合体组合的分析.
主要成果:
- 发现SEC61,SEC62和SEC63中的突变会阻止蛋白质进口到ER光层.
- 基因序列SEC62和SEC63可以预测多跨度膜蛋白.
- 生物化学数据证实Sec62是ER膜蛋白的一个组成部分.
- 蛋白质SEC61,SEC62和SEC63与其他两种蛋白质组合成一个多子单元膜关联复合体.
结论:
- 这些SEC61,SEC62和SEC63蛋白质作为一个复合体一起工作.
- 这种多子单元复合体对于促进分泌蛋白转移到ER至关重要.
- 这些发现支持了这些SEC基因在蛋白质进口中协作作用的假设.
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
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...
Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Tail-anchoring of Proteins in the ER Membrane
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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...
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.


