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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Kannangara R,Siukstaite L,Borch-Jensen J,Madsen B,Kongstad KT,Staerk D,Bennedsen M,Okkels FT,Rasmussen SA,Larsen TO,Frandsen RJN,Møller BLdoi
10.1038/s41467-017-02031-zsubject
Has Abstractpub_date
2017-12-07 00:00:00pages
1987issue
1issn
2041-1723pii
10.1038/s41467-017-02031-zjournal_volume
8pub_type
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