Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses

Farid, Akhlaq, Malinovsky, Frederikke Gro, Veit, Christiane, Schoberer, Jennifer, Zipfel, Cyril and Strasser, Richard (2013) Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses. Plant Physiology, 162 (1). pp. 24-38. ISSN 0032-0889

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Abstract

Asparagine-linked glycosylation of proteins is an essential cotranslational and posttranslational protein modification in plants. The central step in this process is the transfer of a preassembled oligosaccharide to nascent proteins in the endoplasmic reticulum by the oligosaccharyltransferase (OST) complex. Despite the importance of the catalyzed reaction, the composition and the function of individual OST subunits are still ill defined in plants. Here, we report the function of the highly conserved OST subunit OST3/6. We have identified a mutant in the OST3/6 gene that causes overall underglycosylation of proteins and affects the biogenesis of the receptor kinase EF-TU RECEPTOR involved in innate immunity and the endo-β-1,4-glucanase KORRIGAN1 required for cellulose biosynthesis. Notably, the ost3/6 mutation does not affect mutant variants of the receptor kinase BRASSINOSTEROID-INSENSITIVE1. OST3/6 deficiency results in activation of the unfolded protein response and causes hypersensitivity to salt/osmotic stress and to the glycosylation inhibitor tunicamycin. Consistent with its role in protein glycosylation, OST3/6 resides in the endoplasmic reticulum and interacts with other subunits of the OST complex. Together, our findings reveal the importance of Arabidopsis (Arabidopsis thaliana) OST3/6 for the efficient glycosylation of specific glycoproteins involved in different physiological processes and shed light on the composition and function of the plant OST complex.

Item Type: Article
Uncontrolled Keywords: amino acid sequence,arabidopsis,arabidopsis proteins,cellulase,cellulose,endoplasmic reticulum,glycoproteins,glycosylation,hexosyltransferases,mannitol,membrane proteins,molecular sequence data,mutation,plant immunity,protein interaction mapping,protein kinases,receptors, pattern recognition,recombinant fusion proteins,seedling,sequence alignment,sodium chloride,stress, physiological,tunicamycin
Faculty \ School: Faculty of Science > School of Biological Sciences
University of East Anglia > Faculty of Science > Research Groups > Plant Sciences
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Depositing User: Pure Connector
Date Deposited: 04 Jul 2014 13:43
Last Modified: 25 Jul 2018 09:43
URI: https://ueaeprints.uea.ac.uk/id/eprint/48868
DOI: 10.1104/pp.113.215509

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