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Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation
Plants have duplicate versions of the oxidative pentose phosphate pathway (oxPPP) enzymes with a subset localized to the chloroplast. The chloroplast oxPPP provides NADPH and pentose sugars for multiple metabolic pathways. This study identified two loss-of-function alleles of the Zea mays (maize) ch...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654415/ https://www.ncbi.nlm.nih.gov/pubmed/23530131 http://dx.doi.org/10.1093/jxb/ert082 |
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author | Spielbauer, Gertraud Li, Li Römisch-Margl, Lilla Do, Phuc Thi Fouquet, Romain Fernie, Alisdair R. Eisenreich, Wolfgang Gierl, Alfons Settles, A. Mark |
author_facet | Spielbauer, Gertraud Li, Li Römisch-Margl, Lilla Do, Phuc Thi Fouquet, Romain Fernie, Alisdair R. Eisenreich, Wolfgang Gierl, Alfons Settles, A. Mark |
author_sort | Spielbauer, Gertraud |
collection | PubMed |
description | Plants have duplicate versions of the oxidative pentose phosphate pathway (oxPPP) enzymes with a subset localized to the chloroplast. The chloroplast oxPPP provides NADPH and pentose sugars for multiple metabolic pathways. This study identified two loss-of-function alleles of the Zea mays (maize) chloroplast-localized oxPPP enzyme 6-phosphogluconate dehydrogenase (6PGDH). These mutations caused a rough endosperm seed phenotype with reduced embryo oil and endosperm starch. Genetic translocation experiments showed that pgd3 has separate, essential roles in both endosperm and embryo development. Endosperm metabolite profiling experiments indicated that pgd3 shifts redox-related metabolites and increases reducing sugars similar to starch-biosynthetis mutants. Heavy isotope-labelling experiments indicates that carbon flux into starch is altered in pgd3 mutants. Labelling experiments with a loss of cytosolic 6PGDH did not affect flux into starch. These results support the known role for plastid-localized oxPPP in oil synthesis and argue that amyloplast-localized oxPPP reactions are integral to endosperm starch accumulation in maize kernels. |
format | Online Article Text |
id | pubmed-3654415 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-36544152013-05-17 Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation Spielbauer, Gertraud Li, Li Römisch-Margl, Lilla Do, Phuc Thi Fouquet, Romain Fernie, Alisdair R. Eisenreich, Wolfgang Gierl, Alfons Settles, A. Mark J Exp Bot Research Paper Plants have duplicate versions of the oxidative pentose phosphate pathway (oxPPP) enzymes with a subset localized to the chloroplast. The chloroplast oxPPP provides NADPH and pentose sugars for multiple metabolic pathways. This study identified two loss-of-function alleles of the Zea mays (maize) chloroplast-localized oxPPP enzyme 6-phosphogluconate dehydrogenase (6PGDH). These mutations caused a rough endosperm seed phenotype with reduced embryo oil and endosperm starch. Genetic translocation experiments showed that pgd3 has separate, essential roles in both endosperm and embryo development. Endosperm metabolite profiling experiments indicated that pgd3 shifts redox-related metabolites and increases reducing sugars similar to starch-biosynthetis mutants. Heavy isotope-labelling experiments indicates that carbon flux into starch is altered in pgd3 mutants. Labelling experiments with a loss of cytosolic 6PGDH did not affect flux into starch. These results support the known role for plastid-localized oxPPP in oil synthesis and argue that amyloplast-localized oxPPP reactions are integral to endosperm starch accumulation in maize kernels. Oxford University Press 2013-05 2013-03-25 /pmc/articles/PMC3654415/ /pubmed/23530131 http://dx.doi.org/10.1093/jxb/ert082 Text en © The Author(2) [2013]. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Spielbauer, Gertraud Li, Li Römisch-Margl, Lilla Do, Phuc Thi Fouquet, Romain Fernie, Alisdair R. Eisenreich, Wolfgang Gierl, Alfons Settles, A. Mark Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
title | Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
title_full | Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
title_fullStr | Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
title_full_unstemmed | Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
title_short | Chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
title_sort | chloroplast-localized 6-phosphogluconate dehydrogenase is critical for maize endosperm starch accumulation |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654415/ https://www.ncbi.nlm.nih.gov/pubmed/23530131 http://dx.doi.org/10.1093/jxb/ert082 |
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