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. 2018 Jan 20;69(9):2355–2365. doi: 10.1093/jxb/ery014

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© The Author(s) 2018. Published by Oxford University Press on behalf of the Society for Experimental Biology.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 5. — Rice D14 generates and covalently binds the active form of SLs. (A) 5DS induced the interaction of rice D14 and D3 in the SEC assay. Upper panel: SEC analysis of the interaction between D14 and D3–ASK1 in the presence of 5DS; the elution volumes of the molecular weight markers are indicated above the peaks. Lower panel: SDS–PAGE analysis of peak fractions from the upper panel; M, molecular weight ruler (kDa). (B) Rice D14 hydrolyzed 5DS and generated the C₅H₅O₂ modification on the catalytic residue H297. A quadruply charged peptide (287-TTVEFLQTEGHLPHLSAPSLLAQVLR-312) of D14 with the 5DS-derived C₅H₅O₂ modification on H297 was identified by MS/MS (m/z=739.40202). The modified peptide was isolated from the trypsin digestion products of D14 in the 5DS-induced D14–D3–ASK1 complex collected in SEC (A). Labeled peaks correspond to masses of y and b ions of the peptide displayed on the top, respectively. The asterisked ‘H’ indicates the modified H297.