Department of Microbiology, The Ohio State University, Columbus, Ohio, USA.
Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA.
mBio. 2017 Aug 1;8(4):e01056-17. doi: 10.1128/mBio.01056-17.
Bacterial elongation factor P (EF-P) plays a pivotal role in the translation of polyproline motifs. To stimulate peptide bond formation, EF-P must enter the ribosome via an empty E-site. Using fluorescence-based single-molecule tracking, Mohapatra et al. (S. Mohapatra, H. Choi, X. Ge, S. Sanyal, and J. C. Weisshaar, mBio 8:e00300-17, 2017, https://doi.org/10.1128/mBio.00300-17) monitored the cellular distribution of EF-P and quantified the frequency of association between EF-P and the ribosome under various conditions. Findings from the study showed that EF-P has a localization pattern that is strikingly similar to that of ribosomes. Intriguingly, EF-P was seen to bind ribosomes more frequently than the estimated number of pausing events, indicating that E-site vacancies occur even when ribosomes are not paused. The study provides new insights into the mechanism of EF-P-dependent peptide bond formation and the intricacies of translation elongation.
细菌延伸因子 P（EF-P）在多脯氨酸基序的翻译中起着关键作用。为了刺激肽键形成，EF-P 必须通过空的 E 位进入核糖体。Mohapatra 等人（S. Mohapatra、H. Choi、X. Ge、S. Sanyal 和 J. C. Weisshaar，mBio 8:e00300-17, 2017, https://doi.org/10.1128/mBio.00300-17）使用基于荧光的单分子追踪技术，监测了 EF-P 的细胞分布，并在各种条件下量化了 EF-P 与核糖体之间的关联频率。研究结果表明，EF-P 的定位模式与核糖体非常相似。有趣的是，EF-P 与核糖体结合的频率高于估计的暂停事件数量，这表明即使核糖体没有暂停，E 位空位也会发生。该研究为 EF-P 依赖性肽键形成的机制和翻译延伸的复杂性提供了新的见解。
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