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Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis
The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 (H68) is a key element in the protein synthesis process, as it coordinates the coupled movements of th...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Microbiology
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9040758/ https://www.ncbi.nlm.nih.gov/pubmed/35348349 http://dx.doi.org/10.1128/mbio.00306-22 |
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author | Cimicata, Giuseppe Fridkin, Gil Bose, Tanaya Eyal, Zohar Halfon, Yehuda Breiner-Goldstein, Elinor Fox, Tara Zimmerman, Ella Bashan, Anat de Val, Natalia Wlodawer, Alexander Yonath, Ada |
author_facet | Cimicata, Giuseppe Fridkin, Gil Bose, Tanaya Eyal, Zohar Halfon, Yehuda Breiner-Goldstein, Elinor Fox, Tara Zimmerman, Ella Bashan, Anat de Val, Natalia Wlodawer, Alexander Yonath, Ada |
author_sort | Cimicata, Giuseppe |
collection | PubMed |
description | The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 (H68) is a key element in the protein synthesis process, as it coordinates the coupled movements of the actors involved in translocation, including the tRNAs and L1 stalk. Examination of cryo-electron microscopy (cryo-EM) structures of ribosomes incubated for various time durations at physiological temperatures led to the identification of functionally relevant H68 movements. These movements assist the transition of the L1 stalk between its open and closed states. H68 spatial flexibility and its significance to the protein synthesis process were confirmed through its effective targeting with antisense PNA oligomers. Our results suggest that H68 is actively involved in ribosome movements that are central to the elongation process. |
format | Online Article Text |
id | pubmed-9040758 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Society for Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-90407582022-04-27 Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis Cimicata, Giuseppe Fridkin, Gil Bose, Tanaya Eyal, Zohar Halfon, Yehuda Breiner-Goldstein, Elinor Fox, Tara Zimmerman, Ella Bashan, Anat de Val, Natalia Wlodawer, Alexander Yonath, Ada mBio Research Article The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 (H68) is a key element in the protein synthesis process, as it coordinates the coupled movements of the actors involved in translocation, including the tRNAs and L1 stalk. Examination of cryo-electron microscopy (cryo-EM) structures of ribosomes incubated for various time durations at physiological temperatures led to the identification of functionally relevant H68 movements. These movements assist the transition of the L1 stalk between its open and closed states. H68 spatial flexibility and its significance to the protein synthesis process were confirmed through its effective targeting with antisense PNA oligomers. Our results suggest that H68 is actively involved in ribosome movements that are central to the elongation process. American Society for Microbiology 2022-03-29 /pmc/articles/PMC9040758/ /pubmed/35348349 http://dx.doi.org/10.1128/mbio.00306-22 Text en Copyright © 2022 Cimicata et al. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Research Article Cimicata, Giuseppe Fridkin, Gil Bose, Tanaya Eyal, Zohar Halfon, Yehuda Breiner-Goldstein, Elinor Fox, Tara Zimmerman, Ella Bashan, Anat de Val, Natalia Wlodawer, Alexander Yonath, Ada Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis |
title | Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis |
title_full | Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis |
title_fullStr | Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis |
title_full_unstemmed | Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis |
title_short | Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis |
title_sort | structural studies reveal the role of helix 68 in the elongation step of protein biosynthesis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9040758/ https://www.ncbi.nlm.nih.gov/pubmed/35348349 http://dx.doi.org/10.1128/mbio.00306-22 |
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