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

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 glucosylatio...

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Autores principales: Kannangara, Rubini, Siukstaite, Lina, Borch-Jensen, Jonas, Madsen, Bjørn, Kongstad, Kenneth T., Staerk, Dan, Bennedsen, Mads, Okkels, Finn T., Rasmussen, Silas A., Larsen, Thomas O., Frandsen, Rasmus J. N., Møller, Birger Lindberg
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5719414/
https://www.ncbi.nlm.nih.gov/pubmed/29215010
http://dx.doi.org/10.1038/s41467-017-02031-z
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author Kannangara, Rubini
Siukstaite, Lina
Borch-Jensen, Jonas
Madsen, Bjørn
Kongstad, Kenneth T.
Staerk, Dan
Bennedsen, Mads
Okkels, Finn T.
Rasmussen, Silas A.
Larsen, Thomas O.
Frandsen, Rasmus J. N.
Møller, Birger Lindberg
author_facet Kannangara, Rubini
Siukstaite, Lina
Borch-Jensen, Jonas
Madsen, Bjørn
Kongstad, Kenneth T.
Staerk, Dan
Bennedsen, Mads
Okkels, Finn T.
Rasmussen, Silas A.
Larsen, Thomas O.
Frandsen, Rasmus J. N.
Møller, Birger Lindberg
author_sort Kannangara, Rubini
collection PubMed
description 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.
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spelling pubmed-57194142017-12-08 Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa Kannangara, Rubini Siukstaite, Lina Borch-Jensen, Jonas Madsen, Bjørn Kongstad, Kenneth T. Staerk, Dan Bennedsen, Mads Okkels, Finn T. Rasmussen, Silas A. Larsen, Thomas O. Frandsen, Rasmus J. N. Møller, Birger Lindberg Nat Commun Article 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. Nature Publishing Group UK 2017-12-07 /pmc/articles/PMC5719414/ /pubmed/29215010 http://dx.doi.org/10.1038/s41467-017-02031-z Text en © 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/.
spellingShingle Article
Kannangara, Rubini
Siukstaite, Lina
Borch-Jensen, Jonas
Madsen, Bjørn
Kongstad, Kenneth T.
Staerk, Dan
Bennedsen, Mads
Okkels, Finn T.
Rasmussen, Silas A.
Larsen, Thomas O.
Frandsen, Rasmus J. N.
Møller, Birger Lindberg
Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa
title Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa
title_full Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa
title_fullStr Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa
title_full_unstemmed Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa
title_short Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa
title_sort characterization of a membrane-bound c-glucosyltransferase responsible for carminic acid biosynthesis in dactylopius coccus costa
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5719414/
https://www.ncbi.nlm.nih.gov/pubmed/29215010
http://dx.doi.org/10.1038/s41467-017-02031-z
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