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Structure – function study of Arabidopsis thaliana core alpha1,3-fucosyltransferase (FucTA)

Abstract : This work brings an insight on conserved motifs and sequence similarities of alpha1,3/4-fucosyltransferases with emphasis on plant core alpha1,3-fucosyltransferases. Core alpha1,3-fucosylation is a conserved feature of plant and invertebrate N-linked oligosaccharides with no yet known biological function. Core alpha1,3-fucosyltransferase activity is connected to pollen, food and insect allergies in many patients. Core alpha1,3-fucose is recognised by the immune system as foreign element, since mammals do not produce this epitope. I present the results of biochemical characterisation (such as divalent metal ion dependency and Km for the donor substrate), protein truncation (deletion of the proposed most C-terminal subdomain unique to plant core alpha1,3-fucosyltransferases), protein fusions (of immuno-detection epitopes and His-tag), and site-directed mutagenesis of Arabidopsis thaliana core alpha1,3-fucosyltransferase A (FucTA). Mutagenesis was carried out by alanine replacement of potentially important residues based on our results of bioinformatics analyses and homology modelling (which is also subject of this work). Alanine screening was performed either to investigate the importance of some residues of the donor substrate binding pocket of A. thaliana FucTA or its putative N-glycosylation sites. The latter study was complemented also with mass spectral fingerprinting.
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Contributor : Peter Both <>
Submitted on : Thursday, January 21, 2010 - 4:09:27 PM
Last modification on : Friday, November 6, 2020 - 4:10:33 AM
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  • HAL Id : tel-00449431, version 1



Peter Both. Structure – function study of Arabidopsis thaliana core alpha1,3-fucosyltransferase (FucTA). Biomolecules [q-bio.BM]. Université Joseph-Fourier - Grenoble I, 2009. English. ⟨tel-00449431⟩



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