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Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation
Bioinformatic analysis indicates that sucrose phosphate synthase (SPS) contains a putative C-terminal sucrose phosphate phosphatase (SPP)-like domain that may facilitates the binding of SPP. If an SPS–SPP enzyme complex exists, it may provide sucrose biosynthesis with an additional level of regulati...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493782/ https://www.ncbi.nlm.nih.gov/pubmed/25873678 http://dx.doi.org/10.1093/jxb/erv101 |
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author | Maloney, Victoria J. Park, Ji-Young Unda, Faride Mansfield, Shawn D. |
author_facet | Maloney, Victoria J. Park, Ji-Young Unda, Faride Mansfield, Shawn D. |
author_sort | Maloney, Victoria J. |
collection | PubMed |
description | Bioinformatic analysis indicates that sucrose phosphate synthase (SPS) contains a putative C-terminal sucrose phosphate phosphatase (SPP)-like domain that may facilitates the binding of SPP. If an SPS–SPP enzyme complex exists, it may provide sucrose biosynthesis with an additional level of regulation, forming a direct metabolic channel for sucrose-6-phosphate between these two enzymes. Herein, the formation of an enzyme complex between SPS and SPP was examined, and the results from yeast two-hybrid experiments suggest that there is indeed an association between these proteins. In addition, in planta bioluminescence resonance energy transfer (BRET) was observed in Arabidopsis seedlings, providing physical evidence for a protein interaction in live cells and in real time. Finally, bimolecular fluorescence complementation (BiFC) was employed in an attempt to detect SPS–SPP interactions visually. The findings clearly demonstrated that SPS interacts with SPP and that this interaction impacts soluble carbohydrate pools and affects carbon partitioning to starch. Moreover, a fusion construct between the two genes promotes plant growth in both transgenic Arabidopsis and hybrid poplar. |
format | Online Article Text |
id | pubmed-4493782 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-44937822015-07-09 Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation Maloney, Victoria J. Park, Ji-Young Unda, Faride Mansfield, Shawn D. J Exp Bot Research Paper Bioinformatic analysis indicates that sucrose phosphate synthase (SPS) contains a putative C-terminal sucrose phosphate phosphatase (SPP)-like domain that may facilitates the binding of SPP. If an SPS–SPP enzyme complex exists, it may provide sucrose biosynthesis with an additional level of regulation, forming a direct metabolic channel for sucrose-6-phosphate between these two enzymes. Herein, the formation of an enzyme complex between SPS and SPP was examined, and the results from yeast two-hybrid experiments suggest that there is indeed an association between these proteins. In addition, in planta bioluminescence resonance energy transfer (BRET) was observed in Arabidopsis seedlings, providing physical evidence for a protein interaction in live cells and in real time. Finally, bimolecular fluorescence complementation (BiFC) was employed in an attempt to detect SPS–SPP interactions visually. The findings clearly demonstrated that SPS interacts with SPP and that this interaction impacts soluble carbohydrate pools and affects carbon partitioning to starch. Moreover, a fusion construct between the two genes promotes plant growth in both transgenic Arabidopsis and hybrid poplar. Oxford University Press 2015-07 2015-04-13 /pmc/articles/PMC4493782/ /pubmed/25873678 http://dx.doi.org/10.1093/jxb/erv101 Text en © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Maloney, Victoria J. Park, Ji-Young Unda, Faride Mansfield, Shawn D. Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
title | Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
title_full | Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
title_fullStr | Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
title_full_unstemmed | Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
title_short | Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
title_sort | sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4493782/ https://www.ncbi.nlm.nih.gov/pubmed/25873678 http://dx.doi.org/10.1093/jxb/erv101 |
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