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相关概念视频

Insertion of Single-pass Transmembrane Proteins in the RER01:26

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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...
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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.
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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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,...
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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.
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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
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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...
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膜蛋白序列直接翻译后插入的特点

Ilya A Kalinin1, Hadas Peled-Zehavi1, Alon B D Barshap1

  • 1Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.

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概括

许多膜蛋白 (MPs) 使用后翻译途径进行C端螺旋体插入,由特定的C尾序列和YidC插入酶指导. 这确保了适当的蛋白质折叠,并预防疾病.

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科学领域:

  • 分子生物学分子生物学
  • 蛋白质生物化学 蛋白质生物化学
  • 细胞机制 细胞机制

背景情况:

  • 多延伸膜蛋白 (MP) 需要精确的跨膜螺旋 (TM) 插入才能进行适当的折叠.
  • TM插入通常发生在通过Sec translocon的翻译过程中.
  • 对于C端TM (cTM) 插入的机制仍然不太了解.

研究的目的:

  • 研究MP中C端跨膜螺旋体 (cTM) 的插入机制.
  • 为了确定参与cTM插入的细胞机械和蛋白质特征.
  • 了解cTM插入缺陷在疾病中的影响.

主要方法:

  • 在不同生物体中对MP序列进行比较分析.
  • 在大肠杆菌和人类细胞系中进行变异性研究,以评估cTM插入.
  • 在cTM插入中涉及的插入酶蛋白的识别.

主要成果:

  • 许多MP使用后翻译途径进行cTM插入,绕过Sec的翻译连接.
  • 进化优化了C端尾的水友性和长度,以实现高效的cTM插入.
  • 在C端尾部的突变破坏了cTM插入,导致蛋白质缺陷,功能丧失和遗传疾病.
  • Oxa1家族成员YidC作为E. coli*中cTMs的插酶.
  • C尾突变损害了cTMs和YidC之间的相互作用.

结论:

  • 膜蛋白序列是精细调整的,以与细胞生物发生机制相互作用,以便适当折叠.
  • 由YidC介导的翻译后插入途径对于特定的膜蛋白来说至关重要.
  • 这条通路的缺陷有助于人类遗传疾病.