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DOI10.1073/PNAS.2010179117
Engineering 6-phosphogluconate dehydrogenase improves grain yield in heat-stressed maize
Ribeiro C.; Hennen-Bierwagen T.A.; Myers A.M.; Cline K.; Settles A.M.
发表日期2021
ISSN00278424
起始页码33177
结束页码33185
卷号117期号:52
英文摘要Endosperm starch synthesis is a primary determinant of grain yield and is sensitive to high-temperature stress. The maize chloroplast-localized 6-phosphogluconate dehydrogenase (6PGDH), PGD3, is critical for endosperm starch accumulation. Maize also has two cytosolic isozymes, PGD1 and PGD2, that are not required for kernel development. We found that cytosolic PGD1 and PGD2 isozymes have heat-stable activity, while amyloplast-localized PGD3 activity is labile under heat stress conditions. We targeted heat-stable 6PGDH to endosperm amyloplasts by fusing the Waxy1 chloroplast targeting the peptide coding sequence to the Pgd1 and Pgd2 open reading frames (ORFs). These WPGD1 and WPGD2 fusion proteins import into isolated chloroplasts, demonstrating a functional targeting sequence. Transgenic maize plants expressing WPGD1 and WPGD2 with an endosperm-specific promoter increased 6PGDH activity with enhanced heat stability in vitro. WPGD1 and WPGD2 transgenes complement the pgd3-defective kernel phenotype, indicating the fusion proteins are targeted to the amyloplast. In the field, the WPGD1 and WPGD2 transgenes can mitigate grain yield losses in high–nighttime-temperature conditions by increasing kernel number. These results provide insight into the subcellular distribution of metabolic activities in the endosperm and suggest the amyloplast pentose phosphate pathway is a heat-sensitive step in maize kernel metabolism that contributes to yield loss during heat stress. © 2020 National Academy of Sciences. All rights reserved.
英文关键词Grain yield; Heat stability; Maize; Pentose phosphate pathway
语种英语
scopus关键词fusion protein; isoenzyme; PGD1 isozyme; PGD2 isozyme; PGD3 isozyme; phosphogluconate dehydrogenase; unclassified drug; amyloplast; Article; carbon metabolism; chloroplast; climate change; controlled study; cytosol; endosperm; enzyme activity; enzyme engineering; enzyme localization; enzyme stability; grain yield; heat sensitivity; heat stress; high temperature; in vitro study; maize; night; nonhuman; open reading frame; pentose phosphate cycle; phenotype; plastid; priority journal; transgene; transgenic crop
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/179605
作者单位Horticultural Sciences Department, University of Florida, Gainesville, FL 32611, United States; Plant Molecular and Cellular Biology Program, University of Florida, Gainesville, FL 32611, United States; Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, United States; Citrus Research and Education Center, University of Florida, Lake Alfred, FL 33850, United States
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Ribeiro C.,Hennen-Bierwagen T.A.,Myers A.M.,et al. Engineering 6-phosphogluconate dehydrogenase improves grain yield in heat-stressed maize[J],2021,117(52).
APA Ribeiro C.,Hennen-Bierwagen T.A.,Myers A.M.,Cline K.,&Settles A.M..(2021).Engineering 6-phosphogluconate dehydrogenase improves grain yield in heat-stressed maize.Proceedings of the National Academy of Sciences of the United States of America,117(52).
MLA Ribeiro C.,et al."Engineering 6-phosphogluconate dehydrogenase improves grain yield in heat-stressed maize".Proceedings of the National Academy of Sciences of the United States of America 117.52(2021).
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