Cargando…

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)...

Descripción completa

Detalles Bibliográficos
Autores principales: Liu, Yong, Yang, Jing, Ruan, Maosen, Zhang, Huiqin, Wang, Junfeng, Li, Yunyan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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
_version_ 1785120277217148928
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
work_keys_str_mv AT liuyong nmrbasedcharacterizationoftheinteractionbetweenyeastoxa1ctdandribosomes
AT yangjing nmrbasedcharacterizationoftheinteractionbetweenyeastoxa1ctdandribosomes
AT ruanmaosen nmrbasedcharacterizationoftheinteractionbetweenyeastoxa1ctdandribosomes
AT zhanghuiqin nmrbasedcharacterizationoftheinteractionbetweenyeastoxa1ctdandribosomes
AT wangjunfeng nmrbasedcharacterizationoftheinteractionbetweenyeastoxa1ctdandribosomes
AT liyunyan nmrbasedcharacterizationoftheinteractionbetweenyeastoxa1ctdandribosomes