Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase

Jack Egelund Madsen; Iben Damager; Kirsten Faber; C Erik Olsen; Peter Ulvskov; Bent Larsen Petersen

doi:10.1016/j.febslet.2008.08.015

Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase

Jack Egelund Madsen, Iben Damager, Kirsten Faber, C Erik Olsen, Peter Ulvskov, Bent Larsen Petersen

Biomolecular Sciences

33 Citations (Scopus)

Abstract

An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-alpha-d-xylose onto methyl alpha-l-fucoside. The product formed was shown by 1D and 2D (1)H NMR spectroscopy to be Me alpha-d-Xyl-(1,3)-alpha-l-Fuc, which is identical to the proposed target structure in the A-chain of rhamnogalacturonan II. Chemically synthesized methyl l-fucosides derivatized by methyl groups on either the 2-, 3- or 4 position were tested as acceptor substrates but only methyl 4-O-methyl-alpha-l-fucopyranoside acted as an acceptor, although to a lesser extent than methyl alpha-l-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase.

Original language	English
Journal	FEBS Letters
Volume	582
Issue number	21-22
Pages (from-to)	3217-3222
Number of pages	6
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2008.08.015
Publication status	Published - 2008

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10.1016/j.febslet.2008.08.015

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@article{7481fa009eb411dd86a6000ea68e967b,

title = "Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase",

abstract = "An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-alpha-d-xylose onto methyl alpha-l-fucoside. The product formed was shown by 1D and 2D (1)H NMR spectroscopy to be Me alpha-d-Xyl-(1,3)-alpha-l-Fuc, which is identical to the proposed target structure in the A-chain of rhamnogalacturonan II. Chemically synthesized methyl l-fucosides derivatized by methyl groups on either the 2-, 3- or 4 position were tested as acceptor substrates but only methyl 4-O-methyl-alpha-l-fucopyranoside acted as an acceptor, although to a lesser extent than methyl alpha-l-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase.",

author = "Madsen, {Jack Egelund} and Iben Damager and Kirsten Faber and Olsen, {C Erik} and Peter Ulvskov and Petersen, {Bent Larsen}",

note = "Author KEYWORDS: rhamnogalacturonan II; pectin; GT-family-77; xylosyltransferase; Pichia pastoris KEYWORDS Plus: MOLECULAR CHARACTERIZATION; ARABIDOPSIS; BIOSYNTHESIS; XYLOGLUCAN; SYNTHASE; PECTIN; GENES; IDENTIFICATION; FAMILY; GALACTOSYLTRANSFERASE",

year = "2008",

doi = "10.1016/j.febslet.2008.08.015",

language = "English",

volume = "582",

pages = "3217--3222",

journal = "F E B S Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "21-22",

}

TY - JOUR

T1 - Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase

AU - Madsen, Jack Egelund

AU - Damager, Iben

AU - Faber, Kirsten

AU - Olsen, C Erik

AU - Ulvskov, Peter

AU - Petersen, Bent Larsen

N1 - Author KEYWORDS: rhamnogalacturonan II; pectin; GT-family-77; xylosyltransferase; Pichia pastoris KEYWORDS Plus: MOLECULAR CHARACTERIZATION; ARABIDOPSIS; BIOSYNTHESIS; XYLOGLUCAN; SYNTHASE; PECTIN; GENES; IDENTIFICATION; FAMILY; GALACTOSYLTRANSFERASE

PY - 2008

Y1 - 2008

N2 - An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-alpha-d-xylose onto methyl alpha-l-fucoside. The product formed was shown by 1D and 2D (1)H NMR spectroscopy to be Me alpha-d-Xyl-(1,3)-alpha-l-Fuc, which is identical to the proposed target structure in the A-chain of rhamnogalacturonan II. Chemically synthesized methyl l-fucosides derivatized by methyl groups on either the 2-, 3- or 4 position were tested as acceptor substrates but only methyl 4-O-methyl-alpha-l-fucopyranoside acted as an acceptor, although to a lesser extent than methyl alpha-l-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase.

AB - An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-alpha-d-xylose onto methyl alpha-l-fucoside. The product formed was shown by 1D and 2D (1)H NMR spectroscopy to be Me alpha-d-Xyl-(1,3)-alpha-l-Fuc, which is identical to the proposed target structure in the A-chain of rhamnogalacturonan II. Chemically synthesized methyl l-fucosides derivatized by methyl groups on either the 2-, 3- or 4 position were tested as acceptor substrates but only methyl 4-O-methyl-alpha-l-fucopyranoside acted as an acceptor, although to a lesser extent than methyl alpha-l-fucoside. At1g56550 is suggested to encode a rhamnogalacturonan II specific xylosyltransferase.

U2 - 10.1016/j.febslet.2008.08.015

DO - 10.1016/j.febslet.2008.08.015

M3 - Journal article

C2 - 18755189

SN - 0014-5793

VL - 582

SP - 3217

EP - 3222

JO - F E B S Letters

JF - F E B S Letters

IS - 21-22

ER -

Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase

Abstract

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