Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation
© The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.
| Veröffentlicht in: | Journal of experimental botany. - 1985. - 66(2015), 14 vom: 14. Juli, Seite 4383-94 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2015
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| Zugriff auf das übergeordnete Werk: | Journal of experimental botany |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't BRET BiFC biomass cellulose poplar protein–protein interaction sucrose phosphate phosphatase sucrose phosphate synthase mehr... |
| Zusammenfassung: | © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology. 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 |
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| Beschreibung: | Date Completed 05.04.2016 Date Revised 21.03.2022 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1460-2431 |
| DOI: | 10.1093/jxb/erv101 |