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Identification of a binding protein for sesamin and characterization of its roles in plant growth

Sesamin is a furofuran-type lignan that is found abundantly in seeds of Sesamum indicum (sesame) and has been widely accepted as a dietary supplement with positive effects on human health. The biological activity of sesamin in human cells and organs has been analysed extensively, although comparativ...

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Autores principales: Tera, Masayuki, Koyama, Tomotsugu, Murata, Jun, Furukawa, Ayako, Mori, Shoko, Azuma, Toshiaki, Watanabe, Takehiro, Hori, Katsuhito, Okazawa, Atsushi, Kabe, Yasuaki, Suematsu, Makoto, Satake, Honoo, Ono, Eiichiro, Horikawa, Manabu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6570762/
https://www.ncbi.nlm.nih.gov/pubmed/31201340
http://dx.doi.org/10.1038/s41598-019-45003-7
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author Tera, Masayuki
Koyama, Tomotsugu
Murata, Jun
Furukawa, Ayako
Mori, Shoko
Azuma, Toshiaki
Watanabe, Takehiro
Hori, Katsuhito
Okazawa, Atsushi
Kabe, Yasuaki
Suematsu, Makoto
Satake, Honoo
Ono, Eiichiro
Horikawa, Manabu
author_facet Tera, Masayuki
Koyama, Tomotsugu
Murata, Jun
Furukawa, Ayako
Mori, Shoko
Azuma, Toshiaki
Watanabe, Takehiro
Hori, Katsuhito
Okazawa, Atsushi
Kabe, Yasuaki
Suematsu, Makoto
Satake, Honoo
Ono, Eiichiro
Horikawa, Manabu
author_sort Tera, Masayuki
collection PubMed
description Sesamin is a furofuran-type lignan that is found abundantly in seeds of Sesamum indicum (sesame) and has been widely accepted as a dietary supplement with positive effects on human health. The biological activity of sesamin in human cells and organs has been analysed extensively, although comparatively few studies show biological functions for sesamin in planta. Herein we screened sesamin-binding proteins (SBP) from sesame seedling extracts using sesamin-immobilized nano-beads. In subsequent peptide mass fingerprinting analyses, we identified a SBP, Steroleosin B, which is one of the membrane proteins found in oil bodies. In addition, pull-down assays and saturation transfer difference-nuclear magnetic resonance (STD-NMR) experiments demonstrated that sesamin binds directly to recombinant Steroleosin B in vitro. Finally, ectopic accumulations of sesamin and Steroleosin B in transgenic Arabidopsis thaliana plants induced severe growth defects including suppression of leaf expansion and root elongation. Collectively, these results indicate that sesamin influences tissue development in the presence of Steroleosin B.
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spelling pubmed-65707622019-06-24 Identification of a binding protein for sesamin and characterization of its roles in plant growth Tera, Masayuki Koyama, Tomotsugu Murata, Jun Furukawa, Ayako Mori, Shoko Azuma, Toshiaki Watanabe, Takehiro Hori, Katsuhito Okazawa, Atsushi Kabe, Yasuaki Suematsu, Makoto Satake, Honoo Ono, Eiichiro Horikawa, Manabu Sci Rep Article Sesamin is a furofuran-type lignan that is found abundantly in seeds of Sesamum indicum (sesame) and has been widely accepted as a dietary supplement with positive effects on human health. The biological activity of sesamin in human cells and organs has been analysed extensively, although comparatively few studies show biological functions for sesamin in planta. Herein we screened sesamin-binding proteins (SBP) from sesame seedling extracts using sesamin-immobilized nano-beads. In subsequent peptide mass fingerprinting analyses, we identified a SBP, Steroleosin B, which is one of the membrane proteins found in oil bodies. In addition, pull-down assays and saturation transfer difference-nuclear magnetic resonance (STD-NMR) experiments demonstrated that sesamin binds directly to recombinant Steroleosin B in vitro. Finally, ectopic accumulations of sesamin and Steroleosin B in transgenic Arabidopsis thaliana plants induced severe growth defects including suppression of leaf expansion and root elongation. Collectively, these results indicate that sesamin influences tissue development in the presence of Steroleosin B. Nature Publishing Group UK 2019-06-14 /pmc/articles/PMC6570762/ /pubmed/31201340 http://dx.doi.org/10.1038/s41598-019-45003-7 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Tera, Masayuki
Koyama, Tomotsugu
Murata, Jun
Furukawa, Ayako
Mori, Shoko
Azuma, Toshiaki
Watanabe, Takehiro
Hori, Katsuhito
Okazawa, Atsushi
Kabe, Yasuaki
Suematsu, Makoto
Satake, Honoo
Ono, Eiichiro
Horikawa, Manabu
Identification of a binding protein for sesamin and characterization of its roles in plant growth
title Identification of a binding protein for sesamin and characterization of its roles in plant growth
title_full Identification of a binding protein for sesamin and characterization of its roles in plant growth
title_fullStr Identification of a binding protein for sesamin and characterization of its roles in plant growth
title_full_unstemmed Identification of a binding protein for sesamin and characterization of its roles in plant growth
title_short Identification of a binding protein for sesamin and characterization of its roles in plant growth
title_sort identification of a binding protein for sesamin and characterization of its roles in plant growth
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6570762/
https://www.ncbi.nlm.nih.gov/pubmed/31201340
http://dx.doi.org/10.1038/s41598-019-45003-7
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