Effects of N-glycosylation on the folding and structure of plant proteins |
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Authors: | Ceriotti A; Duranti M; Bollini R |
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Institution: | 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 |
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Abstract: | 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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