The ribosome and its role in protein folding: looking through a magnifying glass.
The ribosome and its role in protein folding: looking through a magnifying glass.
复制标题
DOI：
10.1107/s2059798317007446
复制
发表时间：
2017-06-01
期刊：
影响因子：
--
通讯作者：
Orlova EV
中科院分区：
文献类型：
--
作者：
Javed A;Christodoulou J;Cabrita LD;Orlova EV
综述了核糖体上蛋白质共翻译折叠的结构生物学研究进展。蛋白质折叠是细胞活动的基础，它从核糖体上共同开始。在翻译过程中，一条新合成的多肽链进入核糖体出口通道，并在进入细胞环境之前与核糖体元件--排列在通道中的r蛋白和rRNA--积极相互作用。虽然对核糖体的结构和功能的理解已经取得了显着进展，但对新生链（NC）的折叠过程知之甚少。冷冻电子显微镜的进步使出口通道内的NC可视化，允许NC和核糖体之间的相互作用的早期一瞥。一旦它从出口通道进入胞质溶胶，NC（仍然附着在其母体核糖体上）可以获得一系列构象，这些构象可以通过NMR光谱来表征。利用分子动力学模拟中的实验约束，可以描述NC结构的系综。为了描绘共翻译蛋白质折叠的过程，混合结构生物学方法是可预见的，可能提供蛋白质折叠的完整原子描述，因为它发生在核糖体上。
The structural biology of co-translational protein folding on the ribosome is reviewed. Protein folding, a process that underpins cellular activity, begins co-translationally on the ribosome. During translation, a newly synthesized polypeptide chain enters the ribosomal exit tunnel and actively interacts with the ribosome elements – the r-proteins and rRNA that line the tunnel – prior to emerging into the cellular milieu. While understanding of the structure and function of the ribosome has advanced significantly, little is known about the process of folding of the emerging nascent chain (NC). Advances in cryo-electron microscopy are enabling visualization of NCs within the exit tunnel, allowing early glimpses of the interplay between the NC and the ribosome. Once it has emerged from the exit tunnel into the cytosol, the NC (still attached to its parent ribosome) can acquire a range of conformations, which can be characterized by NMR spectroscopy. Using experimental restraints within molecular-dynamics simulations, the ensemble of NC structures can be described. In order to delineate the process of co-translational protein folding, a hybrid structural biology approach is foreseeable, potentially offering a complete atomic description of protein folding as it occurs on the ribosome.