当前位置: X-MOL 学术Science › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Mechanism of membrane-tethered mitochondrial protein synthesis
Science ( IF 56.9 ) Pub Date : 2021-02-19 , DOI: 10.1126/science.abe0763
Yuzuru Itoh 1, 2 , Juni Andréll 1, 2 , Austin Choi 3 , Uwe Richter 4, 5, 6 , Priyanka Maiti 3 , Robert B Best 7 , Antoni Barrientos 3 , Brendan J Battersby 4 , Alexey Amunts 1, 2
Affiliation  

Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo–electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1–like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery.



中文翻译:

膜束缚线粒体蛋白质合成机制

线粒体核糖体(mitoribosomes)与线粒体内膜相连,以促进合成蛋白质的共翻译膜插入。我们报告了具有新生多肽的人线粒体核糖体的冷冻电子显微镜结构,通过三个不同的接触位点与插入酶氧化酶组装体 1 样 (OXA1L) 结合。OXA1L 结合与催化新合成多肽递送的线粒体大亚基中的一系列构象变化相关。该机制依赖于 mL45 在出口通道内的折叠,形成两个特定的收缩位点,限制新生链的螺旋形成。出口和膜之间形成间隙,使新合成的蛋白质能够进入。我们的数据阐明了线粒体核糖体与 OXA1L 插入酶相互作用以耦合蛋白质合成和膜递送的基础。

更新日期:2021-02-19
down
wechat
bug