Document Type
Article
Publication Date
8-1-2017
Abstract
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.
Recommended Citation
Tollerson, R., Witzky, A. and Ibba, M. (2017) Elongation Factor P interactions with the ribosome are independent of pausing. mBio 8, e01056-17. https://doi.org/10.1128/mBio.01056-17
Copyright
The authors
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
This article was originally published in mBio, volume 8, in 2017. https://doi.org/10.1128/mBio.01056-17