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. 2016 Mar 7;171(1):93–109. doi: 10.1104/pp.15.01919

Figure 5.

Figure 5.

Xylan XylT activity of the GFP-Trap-purified proteins from MMs of N. benthamiana leaves coexpressing asparagus IRX9-VENUS, IRX10-VENUS, and IRX14A-VENUS. The activity of untransformed, unpurified native asparagus microsomal membranes (top) was used as a positive control. Three asparagus xylan XylTs (AoIRX9, AoIRX10, and AoIRX14A) fused at the C terminus to VENUS were coexpressed in N. benthamiana leaves, the MMs were extracted and detergent solubilized, and the resulting proteins were enriched by coimmunoprecipitation with a GFP-Trap (bottom). Xylan XylT products were analyzed by RP-HPLC. Numbers above the peaks designate the degree of polymerization of xylooligosaccharides. Xyl5-AA was the acceptor.