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Abstract
The N-linked glycosylation of secretory and membrane proteins is the most complex posttranslational modification known to occur in eukaryotic cells. It has been shown to play critical roles in modulating protein function. Although this important biological process has been extensively studied in mammals, much less is known about this biosynthetic pathway in plants. The enzymes involved in plant N-glycan biosynthesis and processing are still not well defined and the mechanism of their genetic regulation is almost completely unknown. In this paper we describe our first attempt to understand the N-linked glycosylation mechanism in a plant species by using the data generated by the Sugarcane Expressed Sequence Tag (SUCEST) project. The SUCEST database was mined for sugarcane gene products potentially involved in the N-glycosylation pathway. This approach has led to the identification and functional assignment of 90 expressed sequence tag (EST) clusters sharing significant sequence similarity with the enzymes involved in N-glycan biosynthesis and processing. The ESTs identified were also analyzed to establish their relative abundance.
Highlights
As in other eukaryotes, most of the soluble and membrane bound proteins that are synthesized on polyribosomes associated with the endoplasmic reticulum (ER) are glycoproteins, including those proteins which will later be exported to the Golgi apparatus, lysosomes, plasma membrane or extracellular matrix
After the transfer, Glc3Man9GlcNAc2 undergoes trimming of the glucose (Glc) and some of the mannose (Man) residues, first in the ER and in the Golgi apparatus (Figure 2A; for a review see Herscovics, 1999), giving rise to high-mannose-type N-glycans containing from five to nine mannose residues
In this paper we describe our first attempt to better understand the N-linked glycosylation mechanism in plants by mining the Sugarcane Expressed Sequence Tag (SUCEST) project database for sugarcane gene products potentially involved in the N-glycosylation pathway
Summary
As in other eukaryotes, most of the soluble and membrane bound proteins that are synthesized on polyribosomes associated with the endoplasmic reticulum (ER) are glycoproteins, including those proteins which will later be exported to the Golgi apparatus, lysosomes, plasma membrane or extracellular matrix. The glycans attached to glycoproteins contain a variety of sugar residues linked in linear or branched structures that can assume many different conformations. Complex-type plant glycans are rare and were recently identified as containing additional α-1,4-fucose and β-1,3-galactose residues linked to the terminal GlcNAc units.
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