title: A putative Arabidopsis thaliana glycosyltransferase, At4g01220, which is closely related to three plant cell wall-specific xylosyltransferases, is differentially expressed spatially and temporally.
abstract: Plant cell wall polysaccharides are amongst the most complex, heterogeneous and abundant bio-molecules on earth. This makes the biosynthetic enzymes, namely the glycosyltransferases and polysaccharide synthases, important research targets in plant science and biotechnology. As an initial step to characterize At4g01220, a putative Arabidopsis thaliana encoding glycosyltransferases in CAZy GT-family-77 that is similar to three known xylosyltransferases involved in the biosynthesis of the pectic polysaccharide, rhamnogalacturonan II, we conducted an expression analysis. In transgenic Arabidopsis thaliana plants containing a fusion between the At4g01220 promoter and the gusA reporter gene we found the expression to be spatially and developmentally regulated. Analysis of Nicotiana benthamiana transfected with the At2g01220::YFP fusion protein revealed that the fusion protein resided in a Brefeldin A-sensitive compartment consistent with a sub-cellular location in the Golgi apparatus. In addition, in silico expression analysis from the Genevestigator database revealed that At4g01220 was up-regulated upon treatment with isoxaben, an inhibitor of cellulose synthesis, which, together with a co-expression analysis that identified a number of plant cell wall co-related biosynthetic genes, suggests involvement in cell wall biosynthesis with pectin being a prime candidate. The data presented provide insights into the expression, sub-cellular location and regulation of At4g01220 under various conditions and may help elucidate its specific function.
authors.affiliation: Department of Plant Biology and Biotechnology, Faculty of Life Sciences and Centre for Pro-Active Plants (VKR), University of Copenhagen, Thorvaldsensvej 40, Frederiksberg 1871, Denmark.
authors.forename: Jonatan U
authors.initials: JU
authors.lastname: Fangel
authors.forename: Bent L
authors.initials: BL
authors.lastname: Petersen
authors.forename: Niels B
authors.initials: NB
authors.lastname: Jensen
authors.forename: William G T
authors.initials: WG
authors.lastname: Willats
authors.forename: Antony
authors.initials: A
authors.lastname: Bacic
authors.forename: Jack
authors.initials: J
authors.lastname: Egelund
mesh_terms: D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics*; D029681:Arabidopsis Proteins / Q000235:genetics* / Q000378:metabolism; D001549:Benzamides / Q000494:pharmacology; D002473:Cell Wall / Q000378:metabolism*; D002482:Cellulose / Q000096:biosynthesis; D018507:Gene Expression Regulation, Developmental; D018506:Gene Expression Regulation, Plant; D017930:Genes, Reporter; D006056:Golgi Apparatus; D010368:Pectins / Q000096:biosynthesis*; D010430:Pentosyltransferases / Q000235:genetics* / Q000378:metabolism; D030821:Plants, Genetically Modified; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism; D014162:Transfection; D015854:Up-Regulation; D000097608:UDP Xylose-Protein Xylosyltransferase
chemical_list: D029681:Arabidopsis Proteins; D001549:Benzamides; D002482:Cellulose; D010368:Pectins; D010430:Pentosyltransferases; D000097608:UDP Xylose-Protein Xylosyltransferase; C042492:rhamnogalacturonan II; C057467:isoxaben; C567977:At4g01220 protein, Arabidopsis