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Journal of Experimental Botany, Vol 49, 1091-1103, Copyright © 1998 by Oxford University Press

ARTICLES

Effects of N-glycosylation on the folding and structure of plant proteins

A Ceriotti, M Duranti and R Bollini
Istituto Biosintesi Vegetali, Via Bassini 15, I-20133 Milan, Italy; Dipartimento di Scienze Molecolari Agroalimentari, Via Celoria 2, I-20133 Milan, Italy; Corresponding author; e-mail: alce@icm.mi.cnr.it

The synthesis of many of the proteins that are translocated into the endoplasmic reticulum is accompanied by the co-translational attachment of preformed oligosaccharide chains to certain Asn residues. These glycoproteins can play a variety of roles in the mature proteins, including the one of stabilizing the protein and protecting the polypeptide backbone from the action of proteases. In addition, they can have a crucial function during the process of polypeptide folding, when aggregation with other proteins would hamper the acquisition of the native conformation. Their influence on protein folding can be direct, or mediated by interactions with endoplasmic reticulum-located molecular chaperones. The elucidation of the mechanisms that govern glycoprotein folding in the plant endoplasmic reticulum should contribute to the understanding of how much plant cells rely on glycan chains to achieve the efficient folding of many proteins under diverse environmental conditions. In addition, a better knowledge of the level of conservation of the in vivo folding mechanisms will be important for the exploitation of plant cells in the production of heterologous glycoproteins.Keywords: Calnexin, calreticulin, endoplasmic reticulum, glucose trimming, glycoprotein stability.
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