Sucrose phosphate synthase and sucrose phosphate phosphatase interactin plantaand promote plant growth and biomass accumulation
Author(s) -
Victoria Maloney,
Ji Young Park,
Faride Unda,
Shawn D. Mansfield
Publication year - 2015
Publication title -
journal of experimental botany
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.616
H-Index - 242
eISSN - 1460-2431
pISSN - 0022-0957
DOI - 10.1093/jxb/erv101
Subject(s) - sucrose phosphate synthase , bimolecular fluorescence complementation , arabidopsis , biochemistry , sucrose , sugar phosphates , complementation , phosphate , phosphatase , sucrose synthase , enzyme , arabidopsis thaliana , biology , yeast , protein fragment complementation assay , chemistry , invertase , gene , phenotype , mutant
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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