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OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm
Starch is the main storage carbohydrate in higher plants. Although several enzymes and regulators for starch biosynthesis have been characterized, a complete regulatory network for starch synthesis in cereal seeds remains elusive. Here, we report the identification and characterization of the rice B...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5215005/ https://www.ncbi.nlm.nih.gov/pubmed/28054650 http://dx.doi.org/10.1038/srep40124 |
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author | Li, Sanfeng Wei, Xiangjin Ren, Yulong Qiu, Jiehua Jiao, Guiai Guo, Xiuping Tang, Shaoqing Wan, Jianmin Hu, Peisong |
author_facet | Li, Sanfeng Wei, Xiangjin Ren, Yulong Qiu, Jiehua Jiao, Guiai Guo, Xiuping Tang, Shaoqing Wan, Jianmin Hu, Peisong |
author_sort | Li, Sanfeng |
collection | PubMed |
description | Starch is the main storage carbohydrate in higher plants. Although several enzymes and regulators for starch biosynthesis have been characterized, a complete regulatory network for starch synthesis in cereal seeds remains elusive. Here, we report the identification and characterization of the rice Brittle1 (OsBT1) gene, which is expressed specifically in the developing endosperm. The osbt1 mutant showed a white-core endosperm and a significantly lower grain weight than the wild-type. The formation and development of compound starch granules in osbt1 was obviously defective: the amyloplast was disintegrated at early developmental stages and the starch granules were disperse and not compound in the endosperm cells in the centre region of osbt1 seeds. The total starch content and amylose content was decreased and the physicochemical properties of starch were altered. Moreover, the degree of polymerization (DP) of amylopectin in osbt1 was remarkably different from that of wild-type. Map-based cloning of OsBT1 indicated that it encodes a putatively ADP-glucose transporter. OsBT1 coded protein localizes in the amyloplast envelope membrane. Furthermore, the expression of starch synthesis related genes was also altered in the osbt1 mutant. These findings indicate that OsBT1 plays an important role in starch synthesis and the formation of compound starch granules. |
format | Online Article Text |
id | pubmed-5215005 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-52150052017-01-09 OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm Li, Sanfeng Wei, Xiangjin Ren, Yulong Qiu, Jiehua Jiao, Guiai Guo, Xiuping Tang, Shaoqing Wan, Jianmin Hu, Peisong Sci Rep Article Starch is the main storage carbohydrate in higher plants. Although several enzymes and regulators for starch biosynthesis have been characterized, a complete regulatory network for starch synthesis in cereal seeds remains elusive. Here, we report the identification and characterization of the rice Brittle1 (OsBT1) gene, which is expressed specifically in the developing endosperm. The osbt1 mutant showed a white-core endosperm and a significantly lower grain weight than the wild-type. The formation and development of compound starch granules in osbt1 was obviously defective: the amyloplast was disintegrated at early developmental stages and the starch granules were disperse and not compound in the endosperm cells in the centre region of osbt1 seeds. The total starch content and amylose content was decreased and the physicochemical properties of starch were altered. Moreover, the degree of polymerization (DP) of amylopectin in osbt1 was remarkably different from that of wild-type. Map-based cloning of OsBT1 indicated that it encodes a putatively ADP-glucose transporter. OsBT1 coded protein localizes in the amyloplast envelope membrane. Furthermore, the expression of starch synthesis related genes was also altered in the osbt1 mutant. These findings indicate that OsBT1 plays an important role in starch synthesis and the formation of compound starch granules. Nature Publishing Group 2017-01-05 /pmc/articles/PMC5215005/ /pubmed/28054650 http://dx.doi.org/10.1038/srep40124 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Li, Sanfeng Wei, Xiangjin Ren, Yulong Qiu, Jiehua Jiao, Guiai Guo, Xiuping Tang, Shaoqing Wan, Jianmin Hu, Peisong OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
title | OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
title_full | OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
title_fullStr | OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
title_full_unstemmed | OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
title_short | OsBT1 encodes an ADP-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
title_sort | osbt1 encodes an adp-glucose transporter involved in starch synthesis and compound granule formation in rice endosperm |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5215005/ https://www.ncbi.nlm.nih.gov/pubmed/28054650 http://dx.doi.org/10.1038/srep40124 |
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