Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function

The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structur...

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Detalles Bibliográficos
Autores principales: Qiu, Lijuan, Chao, Wen, Zhong, Shan, Ren, An-Jing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9958902/
https://www.ncbi.nlm.nih.gov/pubmed/36834797
http://dx.doi.org/10.3390/ijms24043386
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author Qiu, Lijuan
Chao, Wen
Zhong, Shan
Ren, An-Jing
author_facet Qiu, Lijuan
Chao, Wen
Zhong, Shan
Ren, An-Jing
author_sort Qiu, Lijuan
collection PubMed
description The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed.
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spelling pubmed-99589022023-02-26 Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function Qiu, Lijuan Chao, Wen Zhong, Shan Ren, An-Jing Int J Mol Sci Review The ribosomal protein RPS5 is one of the prime proteins to combine with RNA and belongs to the conserved ribosomal protein family. It plays a substantial role in the process of translation and also has some non-ribosome functions. Despite the enormous studies on the relationship between the structure and function of prokaryotic RPS7, the structure and molecular details of the mechanism of eukaryotic RPS5 remain largely unexplored. This article focuses on the structure of RPS5 and its role in cells and diseases, especially the binding to 18S rRNA. The role of RPS5 in translation initiation and its potential use as targets for liver disease and cancer are discussed. MDPI 2023-02-08 /pmc/articles/PMC9958902/ /pubmed/36834797 http://dx.doi.org/10.3390/ijms24043386 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 Review
Qiu, Lijuan
Chao, Wen
Zhong, Shan
Ren, An-Jing
Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
title Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
title_full Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
title_fullStr Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
title_full_unstemmed Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
title_short Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function
title_sort eukaryotic ribosomal protein s5 of the 40s subunit: structure and function
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9958902/
https://www.ncbi.nlm.nih.gov/pubmed/36834797
http://dx.doi.org/10.3390/ijms24043386
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AT zhongshan eukaryoticribosomalproteins5ofthe40ssubunitstructureandfunction
AT renanjing eukaryoticribosomalproteins5ofthe40ssubunitstructureandfunction

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