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Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome
Archaeal ribosomes have many domain-specific features; however, our understanding of these structures is limited. We present 10 cryo-electron microscopy (cryo-EM) structures of the archaeal ribosome from crenarchaeota Sulfolobus acidocaldarius (Sac) at 2.7–5.7 Å resolution. We observed unstable conf...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10516650/ https://www.ncbi.nlm.nih.gov/pubmed/37604686 http://dx.doi.org/10.1093/nar/gkad661 |
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author | Wang, Ying-Hui Dai, Hong Zhang, Ling Wu, Yun Wang, Jingfen Wang, Chen Xu, Cai-Huang Hou, Hai Yang, Bing Zhu, Yongqun Zhang, Xing Zhou, Jie |
author_facet | Wang, Ying-Hui Dai, Hong Zhang, Ling Wu, Yun Wang, Jingfen Wang, Chen Xu, Cai-Huang Hou, Hai Yang, Bing Zhu, Yongqun Zhang, Xing Zhou, Jie |
author_sort | Wang, Ying-Hui |
collection | PubMed |
description | Archaeal ribosomes have many domain-specific features; however, our understanding of these structures is limited. We present 10 cryo-electron microscopy (cryo-EM) structures of the archaeal ribosome from crenarchaeota Sulfolobus acidocaldarius (Sac) at 2.7–5.7 Å resolution. We observed unstable conformations of H68 and h44 of ribosomal RNA (rRNA) in the subunit structures, which may interfere with subunit association. These subunit structures provided models for 12 rRNA expansion segments and 3 novel r-proteins. Furthermore, the 50S–aRF1 complex structure showed the unique domain orientation of aRF1, possibly explaining P-site transfer RNA (tRNA) release after translation termination. Sac 70S complexes were captured in seven distinct steps of the tRNA translocation reaction, confirming conserved structural features during archaeal ribosome translocation. In aEF2-engaged 70S ribosome complexes, 3D classification of cryo-EM data based on 30S head domain identified two new translocation intermediates with 30S head domain tilted 5–6° enabling its disengagement from the translocated tRNA and its release post-translocation. Additionally, we observed conformational changes to aEF2 during ribosome binding and switching from three different states. Our structural and biochemical data provide new insights into archaeal translation and ribosome translocation. |
format | Online Article Text |
id | pubmed-10516650 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-105166502023-09-23 Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome Wang, Ying-Hui Dai, Hong Zhang, Ling Wu, Yun Wang, Jingfen Wang, Chen Xu, Cai-Huang Hou, Hai Yang, Bing Zhu, Yongqun Zhang, Xing Zhou, Jie Nucleic Acids Res NAR Breakthrough Article Archaeal ribosomes have many domain-specific features; however, our understanding of these structures is limited. We present 10 cryo-electron microscopy (cryo-EM) structures of the archaeal ribosome from crenarchaeota Sulfolobus acidocaldarius (Sac) at 2.7–5.7 Å resolution. We observed unstable conformations of H68 and h44 of ribosomal RNA (rRNA) in the subunit structures, which may interfere with subunit association. These subunit structures provided models for 12 rRNA expansion segments and 3 novel r-proteins. Furthermore, the 50S–aRF1 complex structure showed the unique domain orientation of aRF1, possibly explaining P-site transfer RNA (tRNA) release after translation termination. Sac 70S complexes were captured in seven distinct steps of the tRNA translocation reaction, confirming conserved structural features during archaeal ribosome translocation. In aEF2-engaged 70S ribosome complexes, 3D classification of cryo-EM data based on 30S head domain identified two new translocation intermediates with 30S head domain tilted 5–6° enabling its disengagement from the translocated tRNA and its release post-translocation. Additionally, we observed conformational changes to aEF2 during ribosome binding and switching from three different states. Our structural and biochemical data provide new insights into archaeal translation and ribosome translocation. Oxford University Press 2023-08-22 /pmc/articles/PMC10516650/ /pubmed/37604686 http://dx.doi.org/10.1093/nar/gkad661 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | NAR Breakthrough Article Wang, Ying-Hui Dai, Hong Zhang, Ling Wu, Yun Wang, Jingfen Wang, Chen Xu, Cai-Huang Hou, Hai Yang, Bing Zhu, Yongqun Zhang, Xing Zhou, Jie Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
title | Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
title_full | Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
title_fullStr | Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
title_full_unstemmed | Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
title_short | Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
title_sort | cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome |
topic | NAR Breakthrough Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10516650/ https://www.ncbi.nlm.nih.gov/pubmed/37604686 http://dx.doi.org/10.1093/nar/gkad661 |
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