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. 2017 Dec 7;8:1987. doi: 10.1038/s41467-017-02031-z

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Identification of a Dactylopius coccus FK/KA-specific UGT activity. An isolated microsomal protein fraction and a soluble protein fraction from D. coccus were tested for glucosylation activity in vitro using the flavokermesic acid aglucone and the [¹⁴C]UDP-glucose donor. a Coomassie-stained SDS gel of separated microsomal/soluble protein from D. coccus. b TLC-separated [¹⁴C]-labeled products, formed in vitro and monitored by phosphorimaging. [¹⁴C]UDPG [¹⁴C]UDP-glucose, FK flavokermesic acid, CA carminic acid; − incubation without aglucone substrate. The in vitro formation of [¹⁴C]CA was ascribed to the conversion of kermesic acid that still was bound to the D. coccus microsomes despite numerous wash steps during preparation. c A membrane-bound enzyme activity catalyzing the glucosylation of flavokermesic acid and kermesic acid was partially purified by anion-exchange chromatography after solubilization with reduced Triton X-100 (Supplementary Fig. 1). A fraction eluted with 100 mM NaCl and enriched with flavokermesic acid/kermesic acid-specific glucosylation activity was separated on an SDS gel followed by Coomassie staining. Proteins within the apparent mass region of 50–75 kDa were in-gel digested with trypsin and analyzed by LC-MS/MS. Tryptic peptides of DcUGT2, DcUGT4 and DcUGT5 were identified