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

Rubini Maya Kannangara; Lina Siukstaite; Jonas Borch-Jensen; Bjørn Madsen; Kenneth Thermann Kongstad; Dan Stærk; Mads Bennedsen; Finn T. Okkels; Silas A. Rasmussen; Thomas O. Larsen; Rasmus J.N. Frandsen; Birger Lindberg Møller

doi:10.1038/s41467-017-02031-z

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

Rubini Maya Kannangara, Lina Siukstaite, Jonas Borch-Jensen, Bjørn Madsen, Kenneth Thermann Kongstad, Dan Stærk, Mads Bennedsen, Finn T. Okkels, Silas A. Rasmussen, Thomas O. Larsen, Rasmus J.N. Frandsen, Birger Lindberg Møller

9 Citations (Scopus)

70 Downloads (Pure)

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.

Original language	English
Article number	1987
Journal	Nature Communications
Volume	8
Number of pages	12
ISSN	2041-1723
DOIs	https://doi.org/10.1038/s41467-017-02031-z
Publication status	Published - 1 Dec 2017

Access to Document

10.1038/s41467-017-02031-z

Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus CostaFinal published version, 2.49 MB

Cite this

Kannangara, R. M., Siukstaite, L., Borch-Jensen, J., Madsen, B., Kongstad, K. T., Stærk, D., Bennedsen, M., Okkels, F. T., Rasmussen, S. A., Larsen, T. O., Frandsen, R. J. N., & Møller, B. L. (2017). Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa. Nature Communications, 8, Article 1987. https://doi.org/10.1038/s41467-017-02031-z

Kannangara, RM, Siukstaite, L, Borch-Jensen, J, Madsen, B, Kongstad, KT , Stærk, D, Bennedsen, M, Okkels, FT, Rasmussen, SA, Larsen, TO, Frandsen, RJN & Møller, BL 2017, 'Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa', Nature Communications, vol. 8, 1987. https://doi.org/10.1038/s41467-017-02031-z

@article{6f697219d875488d8ebca1cf838a85da,

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

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.",

author = "Kannangara, {Rubini Maya} and Lina Siukstaite and Jonas Borch-Jensen and Bj{\o}rn Madsen and Kongstad, {Kenneth Thermann} and Dan St{\ae}rk and Mads Bennedsen and Okkels, {Finn T.} and Rasmussen, {Silas A.} and Larsen, {Thomas O.} and Frandsen, {Rasmus J.N.} and M{\o}ller, {Birger Lindberg}",

year = "2017",

month = dec,

day = "1",

doi = "10.1038/s41467-017-02031-z",

language = "English",

volume = "8",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "nature publishing group",

}

TY - JOUR

T1 - Characterization of a membrane-bound C-glucosyltransferase responsible for carminic acid biosynthesis in Dactylopius coccus Costa

AU - Kannangara, Rubini Maya

AU - Siukstaite, Lina

AU - Borch-Jensen, Jonas

AU - Madsen, Bjørn

AU - Kongstad, Kenneth Thermann

AU - Stærk, Dan

AU - Bennedsen, Mads

AU - Okkels, Finn T.

AU - Rasmussen, Silas A.

AU - Larsen, Thomas O.

AU - Frandsen, Rasmus J.N.

AU - Møller, Birger Lindberg

PY - 2017/12/1

Y1 - 2017/12/1

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-017-02031-z

DO - 10.1038/s41467-017-02031-z

M3 - Journal article

C2 - 29215010

SN - 2041-1723

VL - 8

JO - Nature Communications

JF - Nature Communications

M1 - 1987

ER -

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

Abstract

Access to Document

Fingerprint

Cite this