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NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes
In mitochondria, the major subunits of oxidative phosphorylation complexes are translated by the mitochondrial ribosome (mito-ribosome). The correct insertion and assembly of these subunits into the inner mitochondrial membrane (IMM) are facilitated by mitochondrial oxidase assembly protein 1 (Oxa1)...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10572626/ https://www.ncbi.nlm.nih.gov/pubmed/37834108 http://dx.doi.org/10.3390/ijms241914657 |
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author | Liu, Yong Yang, Jing Ruan, Maosen Zhang, Huiqin Wang, Junfeng Li, Yunyan |
author_facet | Liu, Yong Yang, Jing Ruan, Maosen Zhang, Huiqin Wang, Junfeng Li, Yunyan |
author_sort | Liu, Yong |
collection | PubMed |
description | In mitochondria, the major subunits of oxidative phosphorylation complexes are translated by the mitochondrial ribosome (mito-ribosome). The correct insertion and assembly of these subunits into the inner mitochondrial membrane (IMM) are facilitated by mitochondrial oxidase assembly protein 1 (Oxa1) during the translation process. This co-translational insertion process involves an association between the mito-ribosome and the C-terminus of Oxa1 (Oxa1-CTD) Nuclear magnetic resonance (NMR) methods were mainly used to investigate the structural characterization of yeast Oxa1-CTD and its mode of interaction with the E. coli 70S ribosome. Oxa1-CTD forms a transient α-helical structure within the residues P342–Q385, which were reported to form an α-helix when combining with the ribosome. Two conserved contact sites that could interact with the ribosome were further identified. The first site was located on the very end of the N-terminus (V321–I327), and the second one encompassed a stretch of amino acid residues I348–Q370. Based on our discoveries and previous reports, a model has been proposed in which Oxa1-CTD interacts with ribosomes, accompanied by transient-to-stable transitions at the second contact site. These observations may enhance our understanding of the potential role of Oxa1-CTD in facilitating the assembly of oxidative phosphorylation complexes and provide insight into the structural characteristics of Oxa1-CTD. |
format | Online Article Text |
id | pubmed-10572626 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-105726262023-10-14 NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes Liu, Yong Yang, Jing Ruan, Maosen Zhang, Huiqin Wang, Junfeng Li, Yunyan Int J Mol Sci Article In mitochondria, the major subunits of oxidative phosphorylation complexes are translated by the mitochondrial ribosome (mito-ribosome). The correct insertion and assembly of these subunits into the inner mitochondrial membrane (IMM) are facilitated by mitochondrial oxidase assembly protein 1 (Oxa1) during the translation process. This co-translational insertion process involves an association between the mito-ribosome and the C-terminus of Oxa1 (Oxa1-CTD) Nuclear magnetic resonance (NMR) methods were mainly used to investigate the structural characterization of yeast Oxa1-CTD and its mode of interaction with the E. coli 70S ribosome. Oxa1-CTD forms a transient α-helical structure within the residues P342–Q385, which were reported to form an α-helix when combining with the ribosome. Two conserved contact sites that could interact with the ribosome were further identified. The first site was located on the very end of the N-terminus (V321–I327), and the second one encompassed a stretch of amino acid residues I348–Q370. Based on our discoveries and previous reports, a model has been proposed in which Oxa1-CTD interacts with ribosomes, accompanied by transient-to-stable transitions at the second contact site. These observations may enhance our understanding of the potential role of Oxa1-CTD in facilitating the assembly of oxidative phosphorylation complexes and provide insight into the structural characteristics of Oxa1-CTD. MDPI 2023-09-28 /pmc/articles/PMC10572626/ /pubmed/37834108 http://dx.doi.org/10.3390/ijms241914657 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Liu, Yong Yang, Jing Ruan, Maosen Zhang, Huiqin Wang, Junfeng Li, Yunyan NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes |
title | NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes |
title_full | NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes |
title_fullStr | NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes |
title_full_unstemmed | NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes |
title_short | NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes |
title_sort | nmr-based characterization of the interaction between yeast oxa1-ctd and ribosomes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10572626/ https://www.ncbi.nlm.nih.gov/pubmed/37834108 http://dx.doi.org/10.3390/ijms241914657 |
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