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Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice

Plastoquinone-9 (PQ-9) is essential for plant growth and development. Recently, we found that fibrillin5 (FBN5), a plastid lipid binding protein, is an essential structural component of the PQ-9 biosynthetic pathway in Arabidopsis. To investigate the functional conservation of FBN5 in monocots and e...

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Autores principales: Kim, Eun-Ha, Lee, Dae-Woo, Lee, Kyeong-Ryeol, Jung, Su-Jin, Jeon, Jong-Seong, Kim, Hyun Uk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5507956/
https://www.ncbi.nlm.nih.gov/pubmed/28751900
http://dx.doi.org/10.3389/fpls.2017.01197
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author Kim, Eun-Ha
Lee, Dae-Woo
Lee, Kyeong-Ryeol
Jung, Su-Jin
Jeon, Jong-Seong
Kim, Hyun Uk
author_facet Kim, Eun-Ha
Lee, Dae-Woo
Lee, Kyeong-Ryeol
Jung, Su-Jin
Jeon, Jong-Seong
Kim, Hyun Uk
author_sort Kim, Eun-Ha
collection PubMed
description Plastoquinone-9 (PQ-9) is essential for plant growth and development. Recently, we found that fibrillin5 (FBN5), a plastid lipid binding protein, is an essential structural component of the PQ-9 biosynthetic pathway in Arabidopsis. To investigate the functional conservation of FBN5 in monocots and eudicots, we identified OsFBN5, the Arabidopsis FBN5 (AtFBN5) ortholog in rice (Oryza sativa). Homozygous Osfbn5-1 and Osfbn5-2 Tos17 insertion null mutants were smaller than wild type (WT) plants when grown on Murashige and Skoog (MS) medium and died quickly when transplanted to soil in a greenhouse. They accumulated significantly less PQ-9 than WT plants, whereas chlorophyll and carotenoid contents were only mildly affected. The reduced PQ-9 content of the mutants was consistent with their lower maximum photosynthetic efficiency, especially under high light. Overexpression of OsFBN5 complemented the seedling lethal phenotype of the Arabidopsis fbn5-1 mutant and restored PQ-9 and PC-8 (plastochromanol-8) to levels comparable to those in WT Arabidopsis plants. Protein interaction experiments in yeast and mesophyll cells confirmed that OsFBN5 interacts with the rice solanesyl diphosphate synthase OsSPS2 and also with Arabidopsis AtSPS1 and AtSPS2. Our data thus indicate that OsFBN5 is the functional equivalent of AtFBN5 and also suggest that the SPSs–FBN5 complex for synthesis of the solanesyl diphosphate tail in PQ-9 is well conserved in Arabidopsis and rice.
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spelling pubmed-55079562017-07-27 Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice Kim, Eun-Ha Lee, Dae-Woo Lee, Kyeong-Ryeol Jung, Su-Jin Jeon, Jong-Seong Kim, Hyun Uk Front Plant Sci Plant Science Plastoquinone-9 (PQ-9) is essential for plant growth and development. Recently, we found that fibrillin5 (FBN5), a plastid lipid binding protein, is an essential structural component of the PQ-9 biosynthetic pathway in Arabidopsis. To investigate the functional conservation of FBN5 in monocots and eudicots, we identified OsFBN5, the Arabidopsis FBN5 (AtFBN5) ortholog in rice (Oryza sativa). Homozygous Osfbn5-1 and Osfbn5-2 Tos17 insertion null mutants were smaller than wild type (WT) plants when grown on Murashige and Skoog (MS) medium and died quickly when transplanted to soil in a greenhouse. They accumulated significantly less PQ-9 than WT plants, whereas chlorophyll and carotenoid contents were only mildly affected. The reduced PQ-9 content of the mutants was consistent with their lower maximum photosynthetic efficiency, especially under high light. Overexpression of OsFBN5 complemented the seedling lethal phenotype of the Arabidopsis fbn5-1 mutant and restored PQ-9 and PC-8 (plastochromanol-8) to levels comparable to those in WT Arabidopsis plants. Protein interaction experiments in yeast and mesophyll cells confirmed that OsFBN5 interacts with the rice solanesyl diphosphate synthase OsSPS2 and also with Arabidopsis AtSPS1 and AtSPS2. Our data thus indicate that OsFBN5 is the functional equivalent of AtFBN5 and also suggest that the SPSs–FBN5 complex for synthesis of the solanesyl diphosphate tail in PQ-9 is well conserved in Arabidopsis and rice. Frontiers Media S.A. 2017-07-13 /pmc/articles/PMC5507956/ /pubmed/28751900 http://dx.doi.org/10.3389/fpls.2017.01197 Text en Copyright © 2017 Kim, Lee, Lee, Jung, Jeon and Kim. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Kim, Eun-Ha
Lee, Dae-Woo
Lee, Kyeong-Ryeol
Jung, Su-Jin
Jeon, Jong-Seong
Kim, Hyun Uk
Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice
title Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice
title_full Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice
title_fullStr Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice
title_full_unstemmed Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice
title_short Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice
title_sort conserved function of fibrillin5 in the plastoquinone-9 biosynthetic pathway in arabidopsis and rice
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5507956/
https://www.ncbi.nlm.nih.gov/pubmed/28751900
http://dx.doi.org/10.3389/fpls.2017.01197
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