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Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice
The ribosome is the basic machinery for translation, and biogenesis of ribosomes involves many coordinated events. However, knowledge about ribosomal dynamics in higher plants is very limited. This study chose a highly conserved trans-factor, the 60S ribosomal subunit nuclear export adaptor NMD3, to...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4071826/ https://www.ncbi.nlm.nih.gov/pubmed/24723395 http://dx.doi.org/10.1093/jxb/eru150 |
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author | Shi, Yanyun Liu, Xiangling Li, Rui Gao, Yaping Xu, Zuopeng Zhang, Baocai Zhou, Yihua |
author_facet | Shi, Yanyun Liu, Xiangling Li, Rui Gao, Yaping Xu, Zuopeng Zhang, Baocai Zhou, Yihua |
author_sort | Shi, Yanyun |
collection | PubMed |
description | The ribosome is the basic machinery for translation, and biogenesis of ribosomes involves many coordinated events. However, knowledge about ribosomal dynamics in higher plants is very limited. This study chose a highly conserved trans-factor, the 60S ribosomal subunit nuclear export adaptor NMD3, to characterize the mechanism of ribosome biogenesis in the monocot plant Oryza sativa (rice). O. sativa NMD3 (OsNMD3) shares all the common motifs and shuttles between the nucleus and cytoplasm via CRM1/XPO1. A dominant negative form of OsNMD3 with a truncated nuclear localization sequence (OsNMD3(ΔNLS)) was retained in the cytoplasm, consequently interfering with the release of OsNMD3 from pre-60S particles and disturbing the assembly of ribosome subunits. Analyses of the transactivation activity and cellulose biosynthesis level revealed low protein synthesis efficiency in the transgenic plants compared with the wild-type plants. Pharmaceutical treatments demonstrated structural alterations in ribosomes in the transgenic plants. Moreover, global expression profiles of the wild-type and transgenic plants were investigated using the Illumina RNA sequencing approach. These expression profiles suggested that overexpression of OsNMD3(ΔNLS) affected ribosome biogenesis and certain basic pathways, leading to pleiotropic abnormalities in plant growth. Taken together, these results strongly suggest that OsNMD3 is important for ribosome assembly and the maintenance of normal protein synthesis efficiency. |
format | Online Article Text |
id | pubmed-4071826 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-40718262014-06-26 Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice Shi, Yanyun Liu, Xiangling Li, Rui Gao, Yaping Xu, Zuopeng Zhang, Baocai Zhou, Yihua J Exp Bot Research Paper The ribosome is the basic machinery for translation, and biogenesis of ribosomes involves many coordinated events. However, knowledge about ribosomal dynamics in higher plants is very limited. This study chose a highly conserved trans-factor, the 60S ribosomal subunit nuclear export adaptor NMD3, to characterize the mechanism of ribosome biogenesis in the monocot plant Oryza sativa (rice). O. sativa NMD3 (OsNMD3) shares all the common motifs and shuttles between the nucleus and cytoplasm via CRM1/XPO1. A dominant negative form of OsNMD3 with a truncated nuclear localization sequence (OsNMD3(ΔNLS)) was retained in the cytoplasm, consequently interfering with the release of OsNMD3 from pre-60S particles and disturbing the assembly of ribosome subunits. Analyses of the transactivation activity and cellulose biosynthesis level revealed low protein synthesis efficiency in the transgenic plants compared with the wild-type plants. Pharmaceutical treatments demonstrated structural alterations in ribosomes in the transgenic plants. Moreover, global expression profiles of the wild-type and transgenic plants were investigated using the Illumina RNA sequencing approach. These expression profiles suggested that overexpression of OsNMD3(ΔNLS) affected ribosome biogenesis and certain basic pathways, leading to pleiotropic abnormalities in plant growth. Taken together, these results strongly suggest that OsNMD3 is important for ribosome assembly and the maintenance of normal protein synthesis efficiency. Oxford University Press 2014-07 2014-04-10 /pmc/articles/PMC4071826/ /pubmed/24723395 http://dx.doi.org/10.1093/jxb/eru150 Text en © The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Shi, Yanyun Liu, Xiangling Li, Rui Gao, Yaping Xu, Zuopeng Zhang, Baocai Zhou, Yihua Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
title | Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
title_full | Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
title_fullStr | Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
title_full_unstemmed | Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
title_short | Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
title_sort | retention of osnmd3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4071826/ https://www.ncbi.nlm.nih.gov/pubmed/24723395 http://dx.doi.org/10.1093/jxb/eru150 |
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