Arabinogalactan Glycosyltransferases: Enzyme Assay, Protein-Protein Interaction, Subcellular Localization, and Perspectives for Application
Author(s) -
Naomi Geshi
Publication year - 2014
Publication title -
advances in botany
Language(s) - English
Resource type - Journals
eISSN - 2356-6604
pISSN - 2314-7857
DOI - 10.1155/2014/434979
Subject(s) - glycosyltransferase , arabinogalactan , glycan , glycosylation , biochemistry , function (biology) , enzyme , subcellular localization , biology , cell wall , arabidopsis thaliana , nucleotide sugar , microbiology and biotechnology , glycoprotein , chemistry , cytoplasm , gene , mutant
Arabinogalactan proteins (AGPs) are abundant extracellular proteoglycans that are found in most plant species and involved in many cellular processes, such as cell proliferation and survival, pattern formation, and growth, and in plant microbe interaction. AGPs are synthesized by posttranslational O-glycosylation of proteins and attached glycan part often constitutes greater than 90% of the molecule. Subtle altered glycan structures during development have been considered to function as developmental markers on the cell surface, but little is known concerning the molecular mechanisms. My group has been working on glycosylation enzymes (glycosyltransferases) of AGPs to investigate glycan function of the molecule. This review summarizes the recent findings from my group as for AtGalT31A, AtGlcAT14A-C, and AtGalT29A of Arabidopsis thaliana with a specific focus on the (i) biochemical enzyme activities; (ii) subcellular compartments targeted by the glycosyltransferases; and (iii) protein-protein interactions. I also discuss application aspect of glycosyltransferase in improving AGP-based product used in industry, for example, gum arabic
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