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The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice
Pentatricopeptide repeat (PPR) proteins constitute one of the largest protein families in land plants. Recent studies revealed the functions of PPR proteins in organellar RNA metabolism and plant development, but the functions of most PPR proteins, especially PPRs localized in the nucleus, remain la...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6760278/ https://www.ncbi.nlm.nih.gov/pubmed/31087099 http://dx.doi.org/10.1093/jxb/erz226 |
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author | Hao, Yuanyuan Wang, Yunlong Wu, Mingming Zhu, Xiaopin Teng, Xuan Sun, Yinglun Zhu, Jianping Zhang, Yuanyan Jing, Ruonan Lei, Jie Li, Jingfang Bao, Xiuhao Wang, Chunming Wang, Yihua Wan, Jianmin |
author_facet | Hao, Yuanyuan Wang, Yunlong Wu, Mingming Zhu, Xiaopin Teng, Xuan Sun, Yinglun Zhu, Jianping Zhang, Yuanyan Jing, Ruonan Lei, Jie Li, Jingfang Bao, Xiuhao Wang, Chunming Wang, Yihua Wan, Jianmin |
author_sort | Hao, Yuanyuan |
collection | PubMed |
description | Pentatricopeptide repeat (PPR) proteins constitute one of the largest protein families in land plants. Recent studies revealed the functions of PPR proteins in organellar RNA metabolism and plant development, but the functions of most PPR proteins, especially PPRs localized in the nucleus, remain largely unknown. Here, we report the isolation and characterization of a rice mutant named floury and growth retardation1 (fgr1). fgr1 showed floury endosperm with loosely arranged starch grains, decreased starch and amylose contents, and retarded seedling growth. Map-based cloning showed that the mutant phenotype was caused by a single nucleotide substitution in the coding region of Os08g0290000. This gene encodes a nuclear-localized PPR protein, which we named OsNPPR1, that affected mitochondrial function. In vitro SELEX and RNA-EMSAs showed that OsNPPR1 was an RNA protein that bound to the CUCAC motif. Moreover, a number of retained intron (RI) events were detected in fgr1. Thus, OsNPPR1 was involved in regulation of mitochondrial development and/or functions that are important for endosperm development. Our results provide novel insights into coordinated interaction between nuclear-localized PPR proteins and mitochondrial function. |
format | Online Article Text |
id | pubmed-6760278 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-67602782019-10-02 The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice Hao, Yuanyuan Wang, Yunlong Wu, Mingming Zhu, Xiaopin Teng, Xuan Sun, Yinglun Zhu, Jianping Zhang, Yuanyan Jing, Ruonan Lei, Jie Li, Jingfang Bao, Xiuhao Wang, Chunming Wang, Yihua Wan, Jianmin J Exp Bot Research Papers Pentatricopeptide repeat (PPR) proteins constitute one of the largest protein families in land plants. Recent studies revealed the functions of PPR proteins in organellar RNA metabolism and plant development, but the functions of most PPR proteins, especially PPRs localized in the nucleus, remain largely unknown. Here, we report the isolation and characterization of a rice mutant named floury and growth retardation1 (fgr1). fgr1 showed floury endosperm with loosely arranged starch grains, decreased starch and amylose contents, and retarded seedling growth. Map-based cloning showed that the mutant phenotype was caused by a single nucleotide substitution in the coding region of Os08g0290000. This gene encodes a nuclear-localized PPR protein, which we named OsNPPR1, that affected mitochondrial function. In vitro SELEX and RNA-EMSAs showed that OsNPPR1 was an RNA protein that bound to the CUCAC motif. Moreover, a number of retained intron (RI) events were detected in fgr1. Thus, OsNPPR1 was involved in regulation of mitochondrial development and/or functions that are important for endosperm development. Our results provide novel insights into coordinated interaction between nuclear-localized PPR proteins and mitochondrial function. Oxford University Press 2019-09-15 2019-05-14 /pmc/articles/PMC6760278/ /pubmed/31087099 http://dx.doi.org/10.1093/jxb/erz226 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Papers Hao, Yuanyuan Wang, Yunlong Wu, Mingming Zhu, Xiaopin Teng, Xuan Sun, Yinglun Zhu, Jianping Zhang, Yuanyan Jing, Ruonan Lei, Jie Li, Jingfang Bao, Xiuhao Wang, Chunming Wang, Yihua Wan, Jianmin The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice |
title | The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice |
title_full | The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice |
title_fullStr | The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice |
title_full_unstemmed | The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice |
title_short | The nuclear-localized PPR protein OsNPPR1 is important for mitochondrial function and endosperm development in rice |
title_sort | nuclear-localized ppr protein osnppr1 is important for mitochondrial function and endosperm development in rice |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6760278/ https://www.ncbi.nlm.nih.gov/pubmed/31087099 http://dx.doi.org/10.1093/jxb/erz226 |
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