Elongation Factor P Interactions with the Ribosome Are Independent of Pausing

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. Sa...

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Autores principales:	Rodney Tollerson, Anne Witzky, Michael Ibba
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	elongation factor P pausing translation Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/a9be95e96cc84002934221dbd0b0f272
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spelling	oai:doaj.org-article:a9be95e96cc84002934221dbd0b0f2722021-11-15T15:51:45ZElongation Factor P Interactions with the Ribosome Are Independent of Pausing10.1128/mBio.01056-172150-7511https://doaj.org/article/a9be95e96cc84002934221dbd0b0f2722017-09-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01056-17https://doaj.org/toc/2150-7511ABSTRACT 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.Rodney TollersonAnne WitzkyMichael IbbaAmerican Society for Microbiologyarticleelongation factor PpausingtranslationMicrobiologyQR1-502ENmBio, Vol 8, Iss 4 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	elongation factor P pausing translation Microbiology QR1-502
spellingShingle	elongation factor P pausing translation Microbiology QR1-502 Rodney Tollerson Anne Witzky Michael Ibba Elongation Factor P Interactions with the Ribosome Are Independent of Pausing
description	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.
format	article
author	Rodney Tollerson Anne Witzky Michael Ibba
author_facet	Rodney Tollerson Anne Witzky Michael Ibba
author_sort	Rodney Tollerson
title	Elongation Factor P Interactions with the Ribosome Are Independent of Pausing
title_short	Elongation Factor P Interactions with the Ribosome Are Independent of Pausing
title_full	Elongation Factor P Interactions with the Ribosome Are Independent of Pausing
title_fullStr	Elongation Factor P Interactions with the Ribosome Are Independent of Pausing
title_full_unstemmed	Elongation Factor P Interactions with the Ribosome Are Independent of Pausing
title_sort	elongation factor p interactions with the ribosome are independent of pausing
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/a9be95e96cc84002934221dbd0b0f272
work_keys_str_mv	AT rodneytollerson elongationfactorpinteractionswiththeribosomeareindependentofpausing AT annewitzky elongationfactorpinteractionswiththeribosomeareindependentofpausing AT michaelibba elongationfactorpinteractionswiththeribosomeareindependentofpausing
_version_	1718427359100534784

Elongation Factor P Interactions with the Ribosome Are Independent of Pausing

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