Fig. 2: SPY can fucosylate itself.

a Overview of an ‘catalytic SPY’/GDP/‘substrate SPY’ complex in the crystal lattice. In SPY dimer A (catalytic SPY), the color coding is the same as in Fig. 1c. In symmetry-related SPY dimer B (substrate SPY), the two protomers are colored in yellow and gray, respectively. A close-up view of the ‘catalytic SPY’ and ‘substrate SPY’ interface is shown in red square. In ‘substrate SPY’ molecule, residues before F20* and in the between of S37* and N44* are invisible in the structure. S21* is located close to the GDP. b Self-fucosylation of full-length SPY and N-termini truncations. Upper panel shows western blotting with biotinylated AAL. Lower panel shows Coomassie blue staining. Experiments were independently repeated three times with similar results. Uncropped images of western blotting membranes and gels are available as source data. c Self-fucosylation of SPY single-point mutants. Upper panel shows western blotting with biotinylated AAL. Lower panel shows Coomassie blue staining. Experiments were independently repeated three times with similar results. Uncropped images of Western blotting membranes and gels are available as source data. d Fucosylation of DELLA by full-length SPY and N-termini truncations. Upper panel shows western blotting with biotinylated AAL. Lower panel shows Coomassie blue staining. Experiments were independently repeated three times with similar results. Uncropped images of western blotting membranes and gels are available as source data. e Fucosylation of DELLA by SPY single-point mutants. Upper panel shows western blotting with biotinylated AAL. Lower panel shows Coomassie blue staining. Experiments were independently repeated three times with similar results. Uncropped images of western blotting membranes and gels are available as source data.