Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II

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Standard

Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II. / Madsen, Jack Egelund; Petersen, Bent Larsen; Motawia, Mohammed Saddik; Damager, Iben; Faik, Ahmed; Olsen, Carl Erik; Ishii, Tadashi; Clausen, Henrik; Ulvskov, Peter; Geshi, Naomi.

In: Plant Cell, Vol. 18, No. 10, 2006, p. 2593-2607.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Madsen, JE, Petersen, BL, Motawia, MS, Damager, I, Faik, A, Olsen, CE, Ishii, T, Clausen, H, Ulvskov, P & Geshi, N 2006, 'Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II', Plant Cell, vol. 18, no. 10, pp. 2593-2607. https://doi.org/10.1105/tpc.105.036566

APA

Madsen, J. E., Petersen, B. L., Motawia, M. S., Damager, I., Faik, A., Olsen, C. E., Ishii, T., Clausen, H., Ulvskov, P., & Geshi, N. (2006). Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II. Plant Cell, 18(10), 2593-2607. https://doi.org/10.1105/tpc.105.036566

Vancouver

Madsen JE, Petersen BL, Motawia MS, Damager I, Faik A, Olsen CE et al. Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II. Plant Cell. 2006;18(10):2593-2607. https://doi.org/10.1105/tpc.105.036566

Author

Madsen, Jack Egelund ; Petersen, Bent Larsen ; Motawia, Mohammed Saddik ; Damager, Iben ; Faik, Ahmed ; Olsen, Carl Erik ; Ishii, Tadashi ; Clausen, Henrik ; Ulvskov, Peter ; Geshi, Naomi. / Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II. In: Plant Cell. 2006 ; Vol. 18, No. 10. pp. 2593-2607.

Bibtex

@article{21356390a1c111ddb6ae000ea68e967b,
title = "Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II",
abstract = "Two homologous plant-specific Arabidopsis thaliana genes, RGXT1 and RGXT2, belong to a new family of glycosyltransferases (CAZy GT-family-77) and encode cell wall (1,3)-alpha-d-xylosyltransferases. The deduced amino acid sequences contain single transmembrane domains near the N terminus, indicative of a type II membrane protein structure. Soluble secreted forms of the corresponding proteins expressed in insect cells showed xylosyltransferase activity, transferring d-xylose from UDP-alpha-d-xylose to l-fucose. The disaccharide product was hydrolyzed by alpha-xylosidase, whereas no reaction was catalyzed by beta-xylosidase. Furthermore, the regio- and stereochemistry of the methyl xylosyl-fucoside was determined by nuclear magnetic resonance to be an alpha-(1,3) linkage, demonstrating the isolated glycosyltransferases to be (1,3)-alpha-d-xylosyltransferases. This particular linkage is only known in rhamnogalacturonan-II, a complex polysaccharide essential to vascular plants, and is conserved across higher plant families. Rhamnogalacturonan-II isolated from both RGXT1 and RGXT2 T-DNA insertional mutants functioned as specific acceptor molecules in the xylosyltransferase assay. Expression of RGXT1- and RGXT2-enhanced green fluorescent protein constructs in Arabidopsis revealed that both fusion proteins were targeted to a Brefeldin A-sensitive compartment and also colocalized with the Golgi marker dye BODIPY TR ceramide, consistent with targeting to the Golgi apparatus. Taken together, these results suggest that RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-d-xylosyltransferases involved in the biosynthesis of pectic rhamnogalacturonan-II.",
author = "Madsen, {Jack Egelund} and Petersen, {Bent Larsen} and Motawia, {Mohammed Saddik} and Iben Damager and Ahmed Faik and Olsen, {Carl Erik} and Tadashi Ishii and Henrik Clausen and Peter Ulvskov and Naomi Geshi",
note = "Keywords: Amino Acid Sequence; Animals; Arabidopsis Proteins; Baculoviridae; Base Sequence; DNA Primers; Golgi Apparatus; Insects; Isoenzymes; Molecular Sequence Data; Pectins; Pentosyltransferases; Reverse Transcriptase Polymerase Chain Reaction; Sequence Homology, Amino Acid; Substrate Specificity",
year = "2006",
doi = "10.1105/tpc.105.036566",
language = "English",
volume = "18",
pages = "2593--2607",
journal = "The Plant Cell",
issn = "1040-4651",
publisher = "American Society of Plant Biologists",
number = "10",

}

RIS

TY - JOUR

T1 - Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II

AU - Madsen, Jack Egelund

AU - Petersen, Bent Larsen

AU - Motawia, Mohammed Saddik

AU - Damager, Iben

AU - Faik, Ahmed

AU - Olsen, Carl Erik

AU - Ishii, Tadashi

AU - Clausen, Henrik

AU - Ulvskov, Peter

AU - Geshi, Naomi

N1 - Keywords: Amino Acid Sequence; Animals; Arabidopsis Proteins; Baculoviridae; Base Sequence; DNA Primers; Golgi Apparatus; Insects; Isoenzymes; Molecular Sequence Data; Pectins; Pentosyltransferases; Reverse Transcriptase Polymerase Chain Reaction; Sequence Homology, Amino Acid; Substrate Specificity

PY - 2006

Y1 - 2006

N2 - Two homologous plant-specific Arabidopsis thaliana genes, RGXT1 and RGXT2, belong to a new family of glycosyltransferases (CAZy GT-family-77) and encode cell wall (1,3)-alpha-d-xylosyltransferases. The deduced amino acid sequences contain single transmembrane domains near the N terminus, indicative of a type II membrane protein structure. Soluble secreted forms of the corresponding proteins expressed in insect cells showed xylosyltransferase activity, transferring d-xylose from UDP-alpha-d-xylose to l-fucose. The disaccharide product was hydrolyzed by alpha-xylosidase, whereas no reaction was catalyzed by beta-xylosidase. Furthermore, the regio- and stereochemistry of the methyl xylosyl-fucoside was determined by nuclear magnetic resonance to be an alpha-(1,3) linkage, demonstrating the isolated glycosyltransferases to be (1,3)-alpha-d-xylosyltransferases. This particular linkage is only known in rhamnogalacturonan-II, a complex polysaccharide essential to vascular plants, and is conserved across higher plant families. Rhamnogalacturonan-II isolated from both RGXT1 and RGXT2 T-DNA insertional mutants functioned as specific acceptor molecules in the xylosyltransferase assay. Expression of RGXT1- and RGXT2-enhanced green fluorescent protein constructs in Arabidopsis revealed that both fusion proteins were targeted to a Brefeldin A-sensitive compartment and also colocalized with the Golgi marker dye BODIPY TR ceramide, consistent with targeting to the Golgi apparatus. Taken together, these results suggest that RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-d-xylosyltransferases involved in the biosynthesis of pectic rhamnogalacturonan-II.

AB - Two homologous plant-specific Arabidopsis thaliana genes, RGXT1 and RGXT2, belong to a new family of glycosyltransferases (CAZy GT-family-77) and encode cell wall (1,3)-alpha-d-xylosyltransferases. The deduced amino acid sequences contain single transmembrane domains near the N terminus, indicative of a type II membrane protein structure. Soluble secreted forms of the corresponding proteins expressed in insect cells showed xylosyltransferase activity, transferring d-xylose from UDP-alpha-d-xylose to l-fucose. The disaccharide product was hydrolyzed by alpha-xylosidase, whereas no reaction was catalyzed by beta-xylosidase. Furthermore, the regio- and stereochemistry of the methyl xylosyl-fucoside was determined by nuclear magnetic resonance to be an alpha-(1,3) linkage, demonstrating the isolated glycosyltransferases to be (1,3)-alpha-d-xylosyltransferases. This particular linkage is only known in rhamnogalacturonan-II, a complex polysaccharide essential to vascular plants, and is conserved across higher plant families. Rhamnogalacturonan-II isolated from both RGXT1 and RGXT2 T-DNA insertional mutants functioned as specific acceptor molecules in the xylosyltransferase assay. Expression of RGXT1- and RGXT2-enhanced green fluorescent protein constructs in Arabidopsis revealed that both fusion proteins were targeted to a Brefeldin A-sensitive compartment and also colocalized with the Golgi marker dye BODIPY TR ceramide, consistent with targeting to the Golgi apparatus. Taken together, these results suggest that RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-d-xylosyltransferases involved in the biosynthesis of pectic rhamnogalacturonan-II.

U2 - 10.1105/tpc.105.036566

DO - 10.1105/tpc.105.036566

M3 - Journal article

C2 - 17056709

VL - 18

SP - 2593

EP - 2607

JO - The Plant Cell

JF - The Plant Cell

SN - 1040-4651

IS - 10

ER -

ID: 8034599