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

Content Provider	Semantic Scholar
Author	Kannangara, Rubini Maya Šiukštaitė, Lina Borch-Jensen, Jonas Madsen, Bjørn Kongstad, Kenneth Thermann Staerk, Dan Bennedsen, Mads Okkels, Finn T. Rasmussen, Silas Anselm Larsen, Thomas Ostenfeld Frandsen, Rasmus J. N. Møller, Birger Lindberg
Copyright Year	2017
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.Carminic acid is a widely applied red colorant that is still harvested from insects because its biosynthesis is not fully understood. Here, the authors identify and characterize a membrane-bound C-glucosyltransferase catalyzing the final step during carminic acid biosynthesis.
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DOI	10.1038/s41467-017-02031-z
PubMed reference number	29215010
Journal	Medline
Volume Number	8
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Alternate Webpage(s)	https://doi.org/10.1038/s41467-017-02031-z
Journal	Nature Communications
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article