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The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice

Members of the Low Phosphate Root (LPR) family have been identified in rice (Oryza sativa) and expression analyses have been conducted. Here, we investigated the functions of one of the five members in rice, LPR5. qRT-PCR and promoter–GUS reporter analyses indicated that under Pi-sufficient conditio...

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Autores principales: Ai, Hao, Cao, Yue, Jain, Ajay, Wang, Xiaowen, Hu, Zhi, Zhao, Gengmao, Hu, Siwen, Shen, Xing, Yan, Yan, Liu, Xiuli, Sun, Yafei, Lan, Xiaoxia, Xu, Guohua, Sun, Shubin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7475252/
https://www.ncbi.nlm.nih.gov/pubmed/32618334
http://dx.doi.org/10.1093/jxb/eraa211
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author Ai, Hao
Cao, Yue
Jain, Ajay
Wang, Xiaowen
Hu, Zhi
Zhao, Gengmao
Hu, Siwen
Shen, Xing
Yan, Yan
Liu, Xiuli
Sun, Yafei
Lan, Xiaoxia
Xu, Guohua
Sun, Shubin
author_facet Ai, Hao
Cao, Yue
Jain, Ajay
Wang, Xiaowen
Hu, Zhi
Zhao, Gengmao
Hu, Siwen
Shen, Xing
Yan, Yan
Liu, Xiuli
Sun, Yafei
Lan, Xiaoxia
Xu, Guohua
Sun, Shubin
author_sort Ai, Hao
collection PubMed
description Members of the Low Phosphate Root (LPR) family have been identified in rice (Oryza sativa) and expression analyses have been conducted. Here, we investigated the functions of one of the five members in rice, LPR5. qRT-PCR and promoter–GUS reporter analyses indicated that under Pi-sufficient conditions OsLPR5 was highly expressed in the roots, and specific expression occurred in the leaf collars and nodes, and its expression was increased under Pi-deficient conditions. In vitro analysis of the purified OsLPR5 protein showed that it exhibited ferroxidase activity. Overexpression of OsLPR5 triggered higher ferroxidase activity, and elevated concentrations of Fe(III) in the xylem sap and of total Fe in the roots and shoots. Transient expression of OsLPR5 in Nicotiana benthamiana provided evidence of its subcellular localization to the cell wall and endoplasmic reticulum. Knockout mutation in OsLPR5 by means of CRISPR-Cas9 resulted in adverse effects on Pi translocation, on the relative expression of Cis-NAT(OsPHO1;2), and on several morphological traits, including root development and yield potential. Our results indicate that ferroxidase-dependent OsLPR5 has both a broad-spectrum influence on growth and development in rice as well as affecting a subset of physiological and molecular traits that govern Pi homeostasis.
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spelling pubmed-74752522020-09-10 The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice Ai, Hao Cao, Yue Jain, Ajay Wang, Xiaowen Hu, Zhi Zhao, Gengmao Hu, Siwen Shen, Xing Yan, Yan Liu, Xiuli Sun, Yafei Lan, Xiaoxia Xu, Guohua Sun, Shubin J Exp Bot Research Papers Members of the Low Phosphate Root (LPR) family have been identified in rice (Oryza sativa) and expression analyses have been conducted. Here, we investigated the functions of one of the five members in rice, LPR5. qRT-PCR and promoter–GUS reporter analyses indicated that under Pi-sufficient conditions OsLPR5 was highly expressed in the roots, and specific expression occurred in the leaf collars and nodes, and its expression was increased under Pi-deficient conditions. In vitro analysis of the purified OsLPR5 protein showed that it exhibited ferroxidase activity. Overexpression of OsLPR5 triggered higher ferroxidase activity, and elevated concentrations of Fe(III) in the xylem sap and of total Fe in the roots and shoots. Transient expression of OsLPR5 in Nicotiana benthamiana provided evidence of its subcellular localization to the cell wall and endoplasmic reticulum. Knockout mutation in OsLPR5 by means of CRISPR-Cas9 resulted in adverse effects on Pi translocation, on the relative expression of Cis-NAT(OsPHO1;2), and on several morphological traits, including root development and yield potential. Our results indicate that ferroxidase-dependent OsLPR5 has both a broad-spectrum influence on growth and development in rice as well as affecting a subset of physiological and molecular traits that govern Pi homeostasis. Oxford University Press 2020-08-06 2020-07-03 /pmc/articles/PMC7475252/ /pubmed/32618334 http://dx.doi.org/10.1093/jxb/eraa211 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Papers
Ai, Hao
Cao, Yue
Jain, Ajay
Wang, Xiaowen
Hu, Zhi
Zhao, Gengmao
Hu, Siwen
Shen, Xing
Yan, Yan
Liu, Xiuli
Sun, Yafei
Lan, Xiaoxia
Xu, Guohua
Sun, Shubin
The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
title The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
title_full The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
title_fullStr The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
title_full_unstemmed The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
title_short The ferroxidase LPR5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
title_sort ferroxidase lpr5 functions in the maintenance of phosphate homeostasis and is required for normal growth and development of rice
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7475252/
https://www.ncbi.nlm.nih.gov/pubmed/32618334
http://dx.doi.org/10.1093/jxb/eraa211
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