Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa

Rubini Kannangara (), Lina Siukstaite, Jonas Borch-Jensen, Bjørn Madsen, Kenneth T. Kongstad, Dan Staerk, Mads Bennedsen, Finn T. Okkels, Silas A. Rasmussen, Thomas O. Larsen, Rasmus J. N. Frandsen and Birger Lindberg Møller ()
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Rubini Kannangara: University of Copenhagen
Lina Siukstaite: University of Copenhagen
Jonas Borch-Jensen: University of Southern Denmark
Bjørn Madsen: Chr. Hansen A/S, Bøge Alle 10-12
Kenneth T. Kongstad: University of Copenhagen
Dan Staerk: University of Copenhagen
Mads Bennedsen: Chr. Hansen A/S, Bøge Alle 10-12
Finn T. Okkels: Chr. Hansen A/S, Bøge Alle 10-12
Silas A. Rasmussen: The Technical University of Denmark
Thomas O. Larsen: The Technical University of Denmark
Rasmus J. N. Frandsen: The Technical University of Denmark
Birger Lindberg Møller: University of Copenhagen

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract Carminic acid, a glucosylated anthraquinone found in scale insects like Dactylopius coccus, has since ancient times been used as a red colorant in various applications. Here we show that a membrane-bound C-glucosyltransferase, isolated from D. coccus and designated DcUGT2, catalyzes the glucosylation of flavokermesic acid and kermesic acid into their respective C-glucosides dcII and carminic acid. DcUGT2 is predicted to be a type I integral endoplasmic reticulum (ER) membrane protein, containing a cleavable N-terminal signal peptide and a C-terminal transmembrane helix that anchors the protein to the ER, followed by a short cytoplasmic tail. DcUGT2 is found to be heavily glycosylated. Truncated DcUGT2 proteins synthesized in yeast indicate the presence of an internal ER-targeting signal. The cleavable N-terminal signal peptide is shown to be essential for the activity of DcUGT2, whereas the transmembrane helix/cytoplasmic domains, although important, are not crucial for its catalytic function.

Date: 2017
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DOI: 10.1038/s41467-017-02031-z

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