Identification and evolution of a plant cell wall specific glycoprotein glycosyl transferase, ExAD

Svenning Rune Möller, Xueying Yi, Silvia Melina Vel?squez, Sascha Gille, Pernille Hansen, Christian Peter Poulsen, Carl Erik Olsen, Martin Rejzek, Harriet Tempé Parsons, Zhang Yang, Hans H. Wandall, Henrik Clausen, Robert A Field, Markus Pauly, Jose M. Estevez, Jesper Harholt, Peter Ulvskov, Bent L Petersen

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Abstract

Extensins are plant cell wall glycoproteins that act as scaffolds for the deposition of the main wall carbohydrate polymers, which are interlocked into the supramolecular wall structure through intra- and inter-molecular iso-di-tyrosine crosslinks within the extensin backbone. In the conserved canonical extensin repeat, Ser-Hyp 4, serine and the consecutive C4-hydroxyprolines (Hyps) are substituted with an α-galactose and 1-5 β- or α-linked arabinofuranoses (Arafs), respectively. These modifications are required for correct extended structure and function of the extensin network. Here, we identified a single Arabidopsis thaliana gene, At3g57630, in clade E of the inverting Glycosyltransferase family GT47 as a candidate for the transfer of Araf to Hyp-arabinofuranotriose (Hyp-β1,4Araf-β1,2Araf-β1,2Araf) side chains in an α-linkage, to yield Hyp-Araf 4 which is exclusively found in extensins. T-DNA knock-out mutants of At3g57630 showed a truncated root hair phenotype, as seen for mutants of all hitherto characterized extensin glycosylation enzymes; both root hair and glycan phenotypes were restored upon reintroduction of At3g57630. At3g57630 was named Extensin Arabinose Deficient transferase, ExAD, accordingly. The occurrence of ExAD orthologs within the Viridiplantae along with its' product, Hyp-Araf 4, point to ExAD being an evolutionary hallmark of terrestrial plants and charophyte green algae.

Original languageEnglish
Article number45341
JournalScientific Reports
Volume7
Number of pages16
ISSN2045-2322
DOIs
Publication statusPublished - 30 Mar 2017

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