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Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation.

Maloney VJ, Park JY, Unda F, Mansfield SD - J. Exp. Bot. (2015)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.

No MeSH data available.


Related in: MedlinePlus

The YFP signal in 5-week-old Nicotiana tabacum cells transiently transformed with BiFC constructs shows interaction between AtSPS and AtSPP proteins. (A) EM–EM negative control, (B) 35SP –YFP positive control, (C) SPS–EM negative control, (D) EM–SPP1 negative control, (E) SPS–SPP1, (F), SPS–SPP2, (G) SPS–SPP3, and (H) SPS–SPP4. Scale bar=20 μm.
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Figure 5: The YFP signal in 5-week-old Nicotiana tabacum cells transiently transformed with BiFC constructs shows interaction between AtSPS and AtSPP proteins. (A) EM–EM negative control, (B) 35SP –YFP positive control, (C) SPS–EM negative control, (D) EM–SPP1 negative control, (E) SPS–SPP1, (F), SPS–SPP2, (G) SPS–SPP3, and (H) SPS–SPP4. Scale bar=20 μm.

Mentions: While the previous yeast two-hybrid and BRET results strongly suggest an interaction between AtSPS and AtSPP, additional evidence was sought by using a BiFC assay to detect AtSPP–AtSPS interactions visually in planta. In BiFC, two proteins that are believed to interact are fused to different non-fluorescent fragments of a fluorescent protein (i.e. YFP) and expressed in live cells. If the proteins of interest do in fact interact, they will facilitate the re-formation of the fluorescent protein enabling it to emit its fluorescent signal which can then be visualized using fluorescence microscopy (Kerppola, 2006). In this study, leaves from 5-week-old N. tabacum were transiently transformed with YN-SPS and either YC-SPP1, 2, 3, or 4. After infiltration with the BiFC-tagged combinations of AtSPS–AtSPPx, leaf tissue was scanned for fluorescence as an indication of AtSPS–AtSPS interactions. 35SP::YFP was used as a positive control while EM–EM, EM–SPPx, and SPS–EM were used as negative controls. It was determined that the optimal time to detect the YFP signal was between 48h and 65h post-infiltration. YFP signal was clearly detected in all of the SPS–SPP lines, providing additional evidence for an interaction between these two proteins (Fig. 5).


Sucrose phosphate synthase and sucrose phosphate phosphatase interact in planta and promote plant growth and biomass accumulation.

Maloney VJ, Park JY, Unda F, Mansfield SD - J. Exp. Bot. (2015)

The YFP signal in 5-week-old Nicotiana tabacum cells transiently transformed with BiFC constructs shows interaction between AtSPS and AtSPP proteins. (A) EM–EM negative control, (B) 35SP –YFP positive control, (C) SPS–EM negative control, (D) EM–SPP1 negative control, (E) SPS–SPP1, (F), SPS–SPP2, (G) SPS–SPP3, and (H) SPS–SPP4. Scale bar=20 μm.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4493782&req=5

Figure 5: The YFP signal in 5-week-old Nicotiana tabacum cells transiently transformed with BiFC constructs shows interaction between AtSPS and AtSPP proteins. (A) EM–EM negative control, (B) 35SP –YFP positive control, (C) SPS–EM negative control, (D) EM–SPP1 negative control, (E) SPS–SPP1, (F), SPS–SPP2, (G) SPS–SPP3, and (H) SPS–SPP4. Scale bar=20 μm.
Mentions: While the previous yeast two-hybrid and BRET results strongly suggest an interaction between AtSPS and AtSPP, additional evidence was sought by using a BiFC assay to detect AtSPP–AtSPS interactions visually in planta. In BiFC, two proteins that are believed to interact are fused to different non-fluorescent fragments of a fluorescent protein (i.e. YFP) and expressed in live cells. If the proteins of interest do in fact interact, they will facilitate the re-formation of the fluorescent protein enabling it to emit its fluorescent signal which can then be visualized using fluorescence microscopy (Kerppola, 2006). In this study, leaves from 5-week-old N. tabacum were transiently transformed with YN-SPS and either YC-SPP1, 2, 3, or 4. After infiltration with the BiFC-tagged combinations of AtSPS–AtSPPx, leaf tissue was scanned for fluorescence as an indication of AtSPS–AtSPS interactions. 35SP::YFP was used as a positive control while EM–EM, EM–SPPx, and SPS–EM were used as negative controls. It was determined that the optimal time to detect the YFP signal was between 48h and 65h post-infiltration. YFP signal was clearly detected in all of the SPS–SPP lines, providing additional evidence for an interaction between these two proteins (Fig. 5).

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Wood Science, University of British Columbia, 2424 Main Mall, Vancouver, BC, V6T 1Z4, Canada.

No MeSH data available.


Related in: MedlinePlus