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Identification and characterization of the first cytokinin glycosyltransferase from rice

BACKGROUND: Cytokinins are one of the five major hormones families in plants and are important for their normal growth and environmental adaptability. In plants, cytokinins are mostly present as glycosides in plants, and their glycosylation modifications are catalyzed by family 1 glycosyltransferase...

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Autores principales: Li, Pan, Lei, Kang, Li, Yanjie, He, Xingrui, Wang, Shuo, Liu, Renmin, Ji, Lusha, Hou, Bingkai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439077/
https://www.ncbi.nlm.nih.gov/pubmed/30923923
http://dx.doi.org/10.1186/s12284-019-0279-9
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author Li, Pan
Lei, Kang
Li, Yanjie
He, Xingrui
Wang, Shuo
Liu, Renmin
Ji, Lusha
Hou, Bingkai
author_facet Li, Pan
Lei, Kang
Li, Yanjie
He, Xingrui
Wang, Shuo
Liu, Renmin
Ji, Lusha
Hou, Bingkai
author_sort Li, Pan
collection PubMed
description BACKGROUND: Cytokinins are one of the five major hormones families in plants and are important for their normal growth and environmental adaptability. In plants, cytokinins are mostly present as glycosides in plants, and their glycosylation modifications are catalyzed by family 1 glycosyltransferases. Current research on cytokinin glycosylation has focused on the biochemical identification of enzymes and the analysis of metabolites in Arabidopsis. There are few studies that examine how cytokinin glycosylation affects its synthesis and accumulation in plants. It is particularly important to understand these processes in food crops such as rice (Oryza sativa); however, to date, cytokinin glycosyltransferase genes in rice have not been reported. RESULTS: In this study, we identified eight rice genes that were functionally homologous to an Arabidopsis cytokinin glycosyltransferase gene. These genes were cloned and expressed in a prokaryotic system to obtain their purified proteins. Through enzymatic analysis and liquid chromatography-mass spectrometry, a single rice glycosyltransferase, Os6, was identified that glycosylated cytokinin in vitro. Os6 was overexpressed in Arabidopsis, and the extraction of cytokinin glycosides showed that Os6 is functionally active in planta. CONCLUSIONS: The identification and characterization of the first cytokinin glycosyltransferase from rice is important for future studies on the cytokinin metabolic pathway in rice. An improved understanding of rice cytokinin glycosyltransferases may facilitate genetic improvements in rice quality. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12284-019-0279-9) contains supplementary material, which is available to authorized users.
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spelling pubmed-64390772019-04-15 Identification and characterization of the first cytokinin glycosyltransferase from rice Li, Pan Lei, Kang Li, Yanjie He, Xingrui Wang, Shuo Liu, Renmin Ji, Lusha Hou, Bingkai Rice (N Y) Original Article BACKGROUND: Cytokinins are one of the five major hormones families in plants and are important for their normal growth and environmental adaptability. In plants, cytokinins are mostly present as glycosides in plants, and their glycosylation modifications are catalyzed by family 1 glycosyltransferases. Current research on cytokinin glycosylation has focused on the biochemical identification of enzymes and the analysis of metabolites in Arabidopsis. There are few studies that examine how cytokinin glycosylation affects its synthesis and accumulation in plants. It is particularly important to understand these processes in food crops such as rice (Oryza sativa); however, to date, cytokinin glycosyltransferase genes in rice have not been reported. RESULTS: In this study, we identified eight rice genes that were functionally homologous to an Arabidopsis cytokinin glycosyltransferase gene. These genes were cloned and expressed in a prokaryotic system to obtain their purified proteins. Through enzymatic analysis and liquid chromatography-mass spectrometry, a single rice glycosyltransferase, Os6, was identified that glycosylated cytokinin in vitro. Os6 was overexpressed in Arabidopsis, and the extraction of cytokinin glycosides showed that Os6 is functionally active in planta. CONCLUSIONS: The identification and characterization of the first cytokinin glycosyltransferase from rice is important for future studies on the cytokinin metabolic pathway in rice. An improved understanding of rice cytokinin glycosyltransferases may facilitate genetic improvements in rice quality. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12284-019-0279-9) contains supplementary material, which is available to authorized users. Springer US 2019-03-29 /pmc/articles/PMC6439077/ /pubmed/30923923 http://dx.doi.org/10.1186/s12284-019-0279-9 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Article
Li, Pan
Lei, Kang
Li, Yanjie
He, Xingrui
Wang, Shuo
Liu, Renmin
Ji, Lusha
Hou, Bingkai
Identification and characterization of the first cytokinin glycosyltransferase from rice
title Identification and characterization of the first cytokinin glycosyltransferase from rice
title_full Identification and characterization of the first cytokinin glycosyltransferase from rice
title_fullStr Identification and characterization of the first cytokinin glycosyltransferase from rice
title_full_unstemmed Identification and characterization of the first cytokinin glycosyltransferase from rice
title_short Identification and characterization of the first cytokinin glycosyltransferase from rice
title_sort identification and characterization of the first cytokinin glycosyltransferase from rice
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439077/
https://www.ncbi.nlm.nih.gov/pubmed/30923923
http://dx.doi.org/10.1186/s12284-019-0279-9
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