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Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site

机译:寡糖基转移酶在转运子结合位点附近的位置直接结合核糖体

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摘要

Oligosaccharyltransferase (OT) transfers high mannose-type gly-cans to the nascent polypeptides that are translated by the membrane-bound ribosome and translocated into the lumen of the endoplasmic reticulum through the Sec61 translocon complex. In this article, we show that purified ribosomes and OT can form a binary complex with a stoichiometry of ≈1 to 1 in the presence of detergent. We present evidence that OT may bind to the large ribosomal subunit near the site where nascent polypeptides exit. We further show that OT and the Sec61 complex can simultaneously bind to ribosomes in vitro. Based on existing data and our findings, we propose that cotranslational translocation and N-glycosylation of nascent polypeptides are mediated by a ternary supramolecular complex consisting of OT, the Sec61 complex, and ribosomes.
机译:寡糖基转移酶(OT)将高甘露糖型糖罐转移至新生的多肽,该多肽经膜结合的核糖体翻译并通过Sec61 translocon复合物转移到内质网腔中。在本文中,我们证明了在去污剂存在下,纯化的核糖体和OT可以形成化学计量约为1:1的二元复合物。我们目前的证据表明,OT可能会结合新生多肽退出的站点附近的大核糖体亚基。我们进一步显示,OT和Sec61复合物可以在体外同时与核糖体结合。根据现有数据和我们的发现,我们提出新生多肽的共翻译易位和N-糖基化是由由OT,Sec61复合物和核糖体组成的三元超分子复合物介导的。

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