Translation machinery captured in motion
| Authors | |
|---|---|
| Year of publication | 2023 |
| Type | Article in Periodical |
| Magazine / Source | Wiley Interdisciplinary Reviews: RNA |
| MU Faculty or unit | |
| Citation | |
| Web | https://wires.onlinelibrary.wiley.com/doi/10.1002/wrna.1792 |
| Doi | http://dx.doi.org/10.1002/wrna.1792 |
| Keywords | cryoelectron microscopy; structural biology; translation |
| Attached files | |
| Description | Translation accuracy is one of the most critical factors for protein synthesis. It is regulated by the ribosome and its dynamic behavior, along with translation factors that direct ribosome rearrangements to make translation a uniform process. Earlier structural studies of the ribosome complex with arrested translation factors laid the foundation for an understanding of ribosome dynamics and the translation process as such. Recent technological advances in time-resolved and ensemble cryo-EM have made it possible to study translation in real time at high resolution. These methods provided a detailed view of translation in bacteria for all three phases: initiation, elongation, and termination. In this review, we focus on translation factors (in some cases GTP activation) and their ability to monitor and respond to ribosome organization to enable efficient and accurate translation.This article is categorized under:Translation > Ribosome Structure/FunctionTranslation > Mechanisms |
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