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Structural and Mechanistic Insights into Protein Translocation

机译:结构和机械洞察蛋白易位

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Many proteins are translocated across the endoplasmic reticulum (ER) membrane in eukaryotes or the plasma membrane in prokaryotes. These proteins use hydrophobic signal sequences or transmembrane (TM) segments to trigger their translocation through the protein-conducting Sec61/SecY channel. Substrates are first directed to the channel by cytosolic targeting factors, which use hydrophobic pockets to bind diverse signal and TM sequences. Subsequently, these hydrophobic sequences insert into the channel, docking into a groove on the outside of the lateral gate of the channel, where they also interact with lipids. Structural data and biochemical experiments have elucidated how channel partners, the ribosome in cotranslational translocation, and the eukaryotic ER chaperone BiP or the prokaryotic cytosolic SecA ATPase in posttranslational translocation move polypeptides unidirectionally across the membrane. Structures of auxiliary components of the bacterial translocon, YidC and SecD/F, provide additional insight. Taken together, these recent advances result in mechanistic models of protein translocation.
机译:许多蛋白质在真核生物中的内质网(ER)膜上兼容,或在原核生物中的血浆膜中。这些蛋白质使用疏水性信号序列或跨膜(TM)段来通过蛋白质导电SEC61 / SECY通道触发它们的易位。底物首先通过细胞溶质靶向因子涉及通道,其使用疏水袋来结合不同的信号和TM序列。随后,这些疏水性序列插入通道中,在通道的横向栅极的外侧切割成凹槽,在那里它们也与脂质相互作用。结构数据和生化实验阐明了通道合作伙伴,核糖体在分类易位中的核糖体,以及在后期易位的后期易位中的真核生物伴侣BIP或原核细胞溶胶SECA ATP酶在膜上单向移动多肽。细菌转运胶囊,YIDC和SECD / F的辅助组分结构提供了额外的洞察力。在一起,最近的前进导致蛋白质易位的机械模型。

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