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Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations
Translation elongation factor EF1A delivers aminoacyl-tRNA to the ribosome in a GTP-bound form, and is released from the ribosome in a GDP-bound form. This association/dissociation cycle proceeds efficiently via a marked conformational change in EF1A. EF1A function is dependent on the ribosomal “sta...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6791870/ https://www.ncbi.nlm.nih.gov/pubmed/31611569 http://dx.doi.org/10.1038/s41598-019-51266-x |
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author | Maruyama, Kei Imai, Hirotatsu Kawamura, Momoko Ishino, Sonoko Ishino, Yoshizumi Ito, Kosuke Uchiumi, Toshio |
author_facet | Maruyama, Kei Imai, Hirotatsu Kawamura, Momoko Ishino, Sonoko Ishino, Yoshizumi Ito, Kosuke Uchiumi, Toshio |
author_sort | Maruyama, Kei |
collection | PubMed |
description | Translation elongation factor EF1A delivers aminoacyl-tRNA to the ribosome in a GTP-bound form, and is released from the ribosome in a GDP-bound form. This association/dissociation cycle proceeds efficiently via a marked conformational change in EF1A. EF1A function is dependent on the ribosomal “stalk” protein of the ribosomal large subunit, although the precise mechanism of action of the stalk on EF1A remains unclear. Here, we clarify the binding mode of archaeal stalk aP1 to GTP-bound aEF1A associated with aPelota. Intriguingly, the C-terminal domain (CTD) of aP1 binds to aEF1A•GTP with a similar affinity to aEF1A•GDP. We have also determined the crystal structure of the aP1-CTD•aEF1A•GTP•aPelota complex at 3.0 Å resolution. The structure shows that aP1-CTD binds to a space between domains 1 and 3 of aEF1A. Biochemical analyses show that this binding is crucial for protein synthesis. Comparison of the structures of aP1-CTD•aEF1A•GTP and aP1-CTD•aEF1A•GDP demonstrates that the binding mode of aP1 changes markedly upon a conformational switch between the GTP- and GDP-bound forms of aEF1A. Taking into account biochemical data, we infer that aP1 employs its structural flexibility to bind to aEF1A before and after GTP hydrolysis for efficient protein synthesis. |
format | Online Article Text |
id | pubmed-6791870 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-67918702019-10-21 Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations Maruyama, Kei Imai, Hirotatsu Kawamura, Momoko Ishino, Sonoko Ishino, Yoshizumi Ito, Kosuke Uchiumi, Toshio Sci Rep Article Translation elongation factor EF1A delivers aminoacyl-tRNA to the ribosome in a GTP-bound form, and is released from the ribosome in a GDP-bound form. This association/dissociation cycle proceeds efficiently via a marked conformational change in EF1A. EF1A function is dependent on the ribosomal “stalk” protein of the ribosomal large subunit, although the precise mechanism of action of the stalk on EF1A remains unclear. Here, we clarify the binding mode of archaeal stalk aP1 to GTP-bound aEF1A associated with aPelota. Intriguingly, the C-terminal domain (CTD) of aP1 binds to aEF1A•GTP with a similar affinity to aEF1A•GDP. We have also determined the crystal structure of the aP1-CTD•aEF1A•GTP•aPelota complex at 3.0 Å resolution. The structure shows that aP1-CTD binds to a space between domains 1 and 3 of aEF1A. Biochemical analyses show that this binding is crucial for protein synthesis. Comparison of the structures of aP1-CTD•aEF1A•GTP and aP1-CTD•aEF1A•GDP demonstrates that the binding mode of aP1 changes markedly upon a conformational switch between the GTP- and GDP-bound forms of aEF1A. Taking into account biochemical data, we infer that aP1 employs its structural flexibility to bind to aEF1A before and after GTP hydrolysis for efficient protein synthesis. Nature Publishing Group UK 2019-10-14 /pmc/articles/PMC6791870/ /pubmed/31611569 http://dx.doi.org/10.1038/s41598-019-51266-x Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Maruyama, Kei Imai, Hirotatsu Kawamura, Momoko Ishino, Sonoko Ishino, Yoshizumi Ito, Kosuke Uchiumi, Toshio Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations |
title | Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations |
title_full | Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations |
title_fullStr | Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations |
title_full_unstemmed | Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations |
title_short | Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations |
title_sort | switch of the interactions between the ribosomal stalk and ef1a in the gtp- and gdp-bound conformations |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6791870/ https://www.ncbi.nlm.nih.gov/pubmed/31611569 http://dx.doi.org/10.1038/s41598-019-51266-x |
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